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Structural Determinants of p53-Independence in Anticancer Ruthenium-Arene Schiff-Base Complexes.
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Article
Structural Determinants of p53-Independence in
Anticancer Ruthenium-Arene Schiff-base Complexes
Mun Juinn Chow, Maria V. Babak, Daniel Yuan Qiang Wong,
Giorgia Pastorin, Christian Gaiddon, and Wee Han Ang
Mol. Pharmaceutics, Just Accepted Manuscript • DOI: 10.1021/acs.molpharmaceut.6b00348 • Publication Date (Web): 13 May 2016
Downloaded from http://pubs.acs.org on May 16, 2016
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Page 1 of 40 Molecular Ph armaceutics
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Structural Determinants of p53-Independence in Anticancer Ruthenium-
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Arene Schiff-base Complexes
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14 Mun Juinn Chow1, 2, Maria V. Babak1, Daniel Yuan Qiang Wong1, Giorgia Pastorin2, 3, Christian
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Gaiddon*4, 5 and Wee Han Ang*,1, 2
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20 1Department of Chemistry, National University of Singapore, 3 Science Drive 3, 117543 Singapore
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23 2NUS Graduate School for Integrative Sciences and Engineering
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26 3Department of Pharmacy, National University of Singapore, 18 Science Drive 4, 117543 Singapore
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29 4U1113 INSERM, 3 Avenue Molière, Strasbourg 67200, France
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5Oncology section, FMTS, Université de Strasbourg, Strasbourg, France
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KEYWORDS
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Ruthenium Arene Schiff-Base Complexes, Anticancer, Structure-Activity Relationship Studies,
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46 p53-independent activity.
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ABSTRACT
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p53 is a key tumor supressor gene involved in key cellular processes and implicated in cancer
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9 therapy. However, it is inactivated in more than 50% of all cancers due to mutation or
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overexpression of its negative regulators. This leads to drug resistance and poor
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chemotherapeutic outcome as most clinical drugs act via a p53-dependent mechanism of action.
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16 An attractive strategy to circumvent this resistance would be to identify new anticancer drugs
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that act via p53-independent mode-of-action. In the present study, we identified 9 Ru (II)-Arene
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Schiff-base (RAS) complexes able to induce p53-independent cytotoxicity and discuss structural
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23 features that are required for their p53-independent activity. Increasing hydrophobicity led to an
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increase in cellular accumulation in cells with a corresponding increase in efficacy. We further
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28 showed that all 9 complexes demonstrated p53-independent activity. This was despite significant
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30 differences in their physicochemical properties suggesting that the iminoquinoline ligand, a
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common structural feature for all the complexes, is required for the p53-independent activity.
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INTRODUCTION
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p53 is a key tumor supressor gene involved in the mediation of cellular DNA repair, cell cycle
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9 arrest, apoptosis-induction and neurotoxicity of anticancer drugs.1-2 It is inactivated in more than
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11 50% of all cancers due to mutation or overexpression of p53 negative regulators.3 As a result,
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these cancers are more resistant to drugs that act via p53-dependent pathways. For instance, p53-
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16 dependent drugs such as oxaliplatin (OXP) or doxorubicin (DOX) are less effective in inducing
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18 apoptosis in these cancer types even after causing significant DNA damage.4-5 Various strategies
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have been explored for more effective treatment of cancers with defective p53 function. One
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23 such strategy involves the resensitization of these cancers to chemotherapy by restoring p53
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activity. This could be done through (i) the inhibition of the interaction between p53 and its
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28 negative regulators or (ii) restoring misfolded mutant p53, using targeted small molecules or
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30 selective peptide sequences.6 However, such treatment is often limited by the off-target effects,
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low efficacy or development of resistance towards these ‘p53-activators’.6-7 A more attractive
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35 strategy would be to identify new anticancer candidates that are able to bypass this resistance
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mechanism entirely by inducing p53-independent antiproliferation.
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The success of Ru (III)-containing compounds such as KP1019, which received favorable
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43 evaluations in preclinical studies,8-9 has lead to recent interest in the development of more active
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45 Ru (II) complexes as anticancer agents.10-12 Some prominent examples of cytotoxic Ru (II)
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complexes that have undergone preclinical studies are RAPTA-C, RM175 and RDC11.13-16
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50 However, many of these Ru (II) complexes have p53-dependent activity and are subjected to the
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same resistance mechanism of p53-mutated cancers. Previous studies indicated that RAPTA-C,
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RM175 and RDC11 induced p53 and its target genes to various degrees.17-19 Many other reported
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57 Ru (II) complexes also exert their antiproliferation effect via p53-dependent pathways.20-26 In
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contrast, only a limited number of Ru (II) complexes have been reported to demonstrate p53-
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independent activity (Fig 1). Several Ru (II)-arene complexes bearing azopyridine,
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8 iminopyridine or chloroquine ligand, and a imidazole-bearing phenanthroline Ru (II) complex
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demonstrated similar toxicity in both wild type colorectal carcinoma HCT116 and p53-null
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13 lineage.27-29 Another Ru (II)-arene complex bearing iminophosphorane ligand induced apoptotic
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15 cell death without p53-induction.30 Other metal complexes of Pt and Os have also been shown to
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act via p53-independent mechanism.27, 31-33 In all cases, the metal centre has little or no influence
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20 on the p53-dependence of these complexes; the p53-independence of these complexes could
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22 often be ‘switched on’ or ‘switched off’ by structural modification to the ligands.27, 33 In light of
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this, a greater understanding of the structural determinents of p53-independence could lead to the
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27 identification of new organoruthenium compounds with p53-independent activity, adding to the
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limited pool of drugs for the effective treatment of resistant cancers with mutated p53 status.
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Previously, a Ru (II)-Arene Schiff-base (RAS) complex bearing 1,3,5-triisopropylbenzene
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35 (TPB) and iminoquinoline ligands, RAS-1T, was identified as a promising lead cytotoxic
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37 compound with an unique mode-of-action.34 Preliminary investigations suggested that RAS-1T
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acted via a mechanism distinct from classical alkylating agents including cisplatin (CDDP) and
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42 other reported anticancer Ru (II) complexes. RAS-1T did not induce p53 overexpression and
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44 was equipotent in epithelial cells BJwt (p53+/+) and BJshp53 (p53-/-). Further investigation of
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47 RAS-1T and its hexamethylbenzene (HMB) analogue, RAS-1H, revealed that both compounds
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49 induced non-apoptotic cell death via ER-stress pathways but the pathways were different for
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each compound.35
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In this work we report a structure-activity relationship study on an expanded set of RAS
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57 complexes that are structurally related to RAS-1H (4) and RAS-1T (5), aimed to (i) investigate
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if p53-independent activity is a general feature of this class of iminoquinoline-containing Ru (II)
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complexes and (ii) identify the key structural features that lead to their p53-independence. We
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8 further discuss their activity against a panel of colorectal (HCT116 and SW480) and gastric
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(AGS and KATOIII) cancer cells, the influence of the arene and chelating ligands on RAS
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13 complexes’ stability to aquation and biological nucleophiles, as well as intracellular
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RESULTS & DISCUSSION
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25 Synthesis and Characterization of RAS Complexes
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28 RAS complexes 1 – 9 (Fig 2) were synthesized using the general reaction route as shown in
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30 Scheme 1. Recently, we reported the synthesis and characterization of 4, 5 and 9.34-35 2-
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33 Quinolinecarboxaldehyde and different aniline derivatives were reacted in dry EtOH or MeOH to
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35 give the bidentate imine ligand with varying degree of purity. Most of the imine ligands could
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not be isolated as pure compounds due to the facile hydrolysis of the imine bond and the crude
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40 product was used directly for synthesis of the RAS complexes by addition of stoichiometric
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42 amount of the corresponding [Ru(η6-arene)Cl ] in MeOH. Complexes 1 – 9 were further
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45 purified and isolated via flash column chromatography. In addition, we report an improved
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47 synthetic protocol of 8 and 9 that did not require purification by column chromatography.
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Briefly, the imine ligand was prepared from 2-quinolinecarboxaldehyde and excess 3-
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52 chloroaniline in toluene using a Dean-Stark apparatus and the crude ligand treated directly with
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54 [Ru(η6-arene)Cl ] in MeOH. The product was filtered through a short plug of neutral alumina
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and recrystallized using vapour diffusion of diethyl ether into a saturated CH Cl solution at 4
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ºC.
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9 The 1H NMR spectra of 1 – 9 showed resonances typical of RAS complexes.34 The
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disappearance of the singlet peak corresponding to quinolinecarboxaldehyde at ca. 10.2 ppm and
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the appearance of the peak corresponding to the imine proton at ca. 8.5-9.5 ppm indicated the
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16 formation of the chelate ligand. The desymmetrization of the Ru complex due to chelation
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resulted in additional splitting pattern of the arene proton signals (arene = toluene, cymene,
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TPB). ESI-MS spectra of these compounds also showed the characteristic [M]+ molecular ion
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23 peaks with Ru and Cl isotopic pattern. The purity of the complexes was confirmed by either
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elemental analysis (EA) or RP-HPLC to be >95%.
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Solid-state structural information was obtained for 4 and 9 via single crystal X-ray diffraction
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31 studies (Fig 3) and selected structural data are given in Table 1 and Table 2. Single crystals
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were obtained via slow diffusion of diethyl ether into saturated CH Cl solution at 4 ºC. RAS
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36 complexes 4 and 9 adopted the classical ‘piano-stool’ structure similar to most reported Ru(II)-
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38 arene complexes with some notable deviations.26, 30, 36 The Ru-C bond ranges for 4 and 9 of
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2.196-2.283 Å and 2.175-2.280 Å, respectively, are longer than RM175 (biphenyl) and RAPTA-
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43 C (cymene) of 2.161-2.231 Å and 2.180-2.262 Å, respectively, presumably due to the sterically
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45 encumbered HMB ligand. All corresponding bond length and angles between 4 and 9 were
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similar, suggesting that changing the 4-OMe group to a 3-Cl group did not alter the core RAS
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50 structure. The conformation adopted by the iminoquinoline ligands could be described by the
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torsion angle θ of 37.6(9)˚ and 34.6(6)˚ for 4 and 9, respectively, disrupting the
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to the steric bulk of the arene ligand. The same structural feature was observed in the recently
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reported RAS complexes.34
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12 Effect of structural variation on stability and Log P
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Aqueous stability and Log P are important factors that affect a potential drug’s
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bioavailability and cell permeability,37 which can potentially influence the molecular target and
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20 mode-of-action. To determine the stability of the 9 RAS complexes under investigation towards
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aquation and biological nucleophiles, we monitored their UV-Vis profile in double distilled H O
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25 (ddH 2 O) and Hanks Balanced Salt Solution (HBSS) containing 10% fetal bovine serum (FBS)
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27 over 24 h. Any reaction would manifest as a shifts in the UV-Vis profile, producing isosbestic
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point(s) in the overlapping spectrums at different time points. The investigated RAS complexes
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32 were generally stable in water (Fig S1). Slight shifts in the spectrums and the formation of
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several isosbestic points were observed for 6, 7 and 8 after 24 h in water, which suggests that the
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aquation of the Ru-Cl bond in 6, 7 and 8 occurred very slowly in the absence of other competing
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39 nucleophiles at r. t..
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42 Although all RAS complexes could be considered to be resistant to aquation in water, only
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some could be considered stable towards interfering nucleophiles as seen in their stability in
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47 serum-containing HBSS (Fig S2). This is particularly well illustrated by focusing on the slight
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variations implemented when comparing 4, 5, 8 and 9 (Fig 4). In general, compounds with more
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52 π-donating arene (HMB, TPB) and less π-acidic iminoquinoline (-OMe) ligands stabilized the
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54 Ru-Cl bonds making it less susceptible towards substitution. For instance, 5 was stable in HBSS
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with 10% FBS. However, changing the 4-OMe to the more π-acidic 3-CF or 3-Cl group (7 and
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8) labilised the Ru-Cl bond. Replacing the TPB arene with the more π-donating HMB in 9
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6 resulted in a more stable complex resistant to Ru-Cl aquation. Furthermore, it cannot be ruled out
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8 that compounds bearing labile benzene or toluene arene ligands (1 and 2) decomposed in serum-
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containing buffer due to the displacement of arene ligand by biological nucleophiles (Fig S2).
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14 Log P OW of 1 – 5 and 9 were determined using the shake-flask method.38 Log P OW of 6, 7 and 8
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phase separation (data not shown), presumably due to non-specific interactions with the n-
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21 octanol phase. The trend in the Log P studies were as expected, where RAS complexes with
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more hydrophobic ligands displayed higher Log P values (Table 3).
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Effects of ligand structural variations on cytotoxicity profile
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33 To determine the effects of structural variation to cytotoxicity, we obtained the IC values of
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the nine RAS complexes in colorectal cancer cell lines HCT116 and SW480, and gastric cancer
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cell lines AGS and KATOIII (Table 3). In general, RAS complexes bearing the more
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40 hydrophobic HMB and TPB arene ligands demonstrated the highest cytotoxicity in the cell lines,
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with IC values in the low µM range. Complex 5 displayed the greatest efficacies with IC ca.
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45 1.0 µM in HCT116, AGS and KATOIII and 4.1 µM in SW480, which was 34- and 7-fold more
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47 cytotoxic than CDDP in AGS and KATOIII, respectively. For RAS complexes with 4-OMe (1 –
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5), IC values decreased with the increasing hydrophobicity of the arene ligand, from the least
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52 hydrophobic benzene in 1 to the most hydrophobic TPB in 5. Interestingly, starting from
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KATOIII, suggesting that hydrophobicity also affected selectivity between different cancer
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types.
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9 Both 4 and 9 demonstrated biphasic dose-response curve in AGS and KATOIII cells,
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respectively. AGS cell viability decreased with increasing concentration of 4 to reach a plateau
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of 40% between 5 µM and 20 µM before dropping drastically to 0% above 20 µM (Fig 5a).34 A
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16 similar biphasic profile was seen in KATOIII cells treated with 9 (Fig 5b). In contrast, the TPB
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analogues (5 and 8) did not display such biphasic dose-response profiles. The basis for this
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unique concentration-dependent mechanism of antiproliferative activity induced by HMB-
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23 bearing RAS complexes (4 and 9) remains to be elucidated. This biphasic dose-response was not
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observed in benzene, toluene, cymene or TPB RAS analogues. Few reported anticancer
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28 compounds exhibit such biphasic dose-response profiles. One such compound is anti-tubule
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apoptosis at higher doses in prostate cancer (PC3, DU145) and breast cancer cell lines (MCF7,
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35 MDA-MB-231).39-42 A similar concentration-dependent dual mode-of-action for 4 and 9 would
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be highly conceivable.
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44 RAS complexes accumulate in cells mainly by passive diffusion
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47 One possibility for the higher cytotoxicity of compounds bearing hydrophobic arene ligands
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49 could be attributed to better cellular uptake via passive diffusion.43 More efficient cellular
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accumulation of the RAS compounds may result in a higher efficacy. The RAS complexes
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investigated whether varying the hydrophobicity of the arene ligands (1 – 5) affected cellular
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uptake in HCT116 cells, with 6 and OXP for comparison. Cell samples were centrifuged,
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washed, and digested separately in concentrated HNO before their Ru/Pt contents were analyzed
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8 by ICP-MS (Table S1).
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There was a positive correlation between hydrophobicity, cellular accumulation and
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cytotoxicity for 1 – 5 (Fig 6a-b). When treated at the same concentration of 1.5 µM, the most
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16 hydrophobic complex 5 accumulated 7.5-times more than 1, the least hydrophobic complex.
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Interestingly, complex 6 accumulated 3 times less than complex 4 but had a higher cytotoxicity.
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Hence, with the exception of complex 6, the higher uptake also corresponded with lower IC
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hydrophobic RAS complexes. In addition, there was an interesting abrupt improvement of drug
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28 intake at a Log P ow just above -1.5, suggesting that this value might be considered as a goal for
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Since the RAS complexes are cationic and bear hydrophobic ligands, we investigated if
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36 organic cation transporters (OCT) could be responsible for their activity in colorectal cancer in a
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38 similar manner as OXP. OXP was effective in the treatment of colorectal cancer compared to
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CDDP and attributed to the fact that OXP was a substrate for OCT1/2 and would be more
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43 efficiently accumulated in OCT-overexpressing colorectal cancer cells.44 As the RAS complexes
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OCTs in a similar fashion to OXP. Hence HCT116 cells were treated with 5 and 6 for 7 h in the
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50 presence and absence of OCT2-inhibitor cimetidine and compared to OXP as a positive control.
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Cimetidine did not affect the viability of cells treated with 5 and 6, suggesting that both are not
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substrates of OCT2 (Fig 7a-b). In contrast, the viability of cells treated with OXP increased in
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57 the presence of cimetidine (Fig 7c), indicating reduced uptake of the cytotoxic OXP. Taken
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together, the data suggested that RAS complexes accumulated in the cell mainly via passive
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diffusion. A general trend indicated that increasing hydrophobicity resulted in increased cellular
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8 uptake and higher toxicity, which was characteristic of entry by passive diffusion. However,
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exception such as in complex 6 indicated that additional mechanisms and physicochemical
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13 determinants might exist and could participate in the uptake process. Although, OCT transporters
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uptake pathways are involved in the cellular accumulation of RAS complexes cannot be
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Structural determinant of p53-Independent mode-of-action
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We determined previously that 4 and 5 induced cell death in AGS and HCT116 cells without
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32 concomitant induction of p53.34-35 To further verify the p53-independence of the RAS
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complexes, we evaluated the expression of p53 as well as downstream, cell cycle-arresting and
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apoptosis-associated biomarkers in treated HCT116 cells. Cells were exposed to 4, 5, 8 and 9 for
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absence and presence of p53-inhibitor pifithrin-α. OXP was used as a positive control.
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Western blot analysis was performed against p53 and its targets, cell cycle-regulating cyclin
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47 D1 and p21 (Fig 8a).45-47 In general, there was a lack of induction of these biomarkers by 4, 5, 8
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and 9 although p53-independent induction of p21 was observed with 4, 5 and 9 after 24 h
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exposure.48 In contrast, OXP exhibited a concentration and time-dependent upregulation of p53,
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54 cyclin D1 and p21. RT-qPCR analyses were performed on p53-regulated anti-apoptotic gene
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56 BCL2 and pro-apoptotic genes NOXA and BAX (Fig 8b).49-51 Complexes 4 and 9 induced a slight
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increase in NOXA expression at the later time points (6 h and 24 h) while 5 and 8 did not cause
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significant change in NOXA expression. Cells treated with 4, 5, 8 and 9 also induced negligible
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8 change in expression of BAX and BCL2. In contrast, OXP treatment at IC led to 3-fold
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induction of NOXA, 5.5-fold increase in BAX and a significant reduction in BCL2 after 24 h
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13 exposure. To demonstrate functionally that the cytotoxic activities of 4, 5, 8 and 9 were
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15 independent of p53, cells were co-incubated with pifithrin-α. Co-treatment of 4, 5, 8 and 9 with
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pifithrin-α improved the efficacies of RAS complexes while in the case of OXP, co-treatment
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20 incurred a 3-fold increase in IC suggesting that OXP exerted its cytotoxicity via a p53-
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dependent pathway.
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The lack of significant induction of p53 and its downstream targets implied that these RAS
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28 complexes exerted their antiproliferative effects via p53-independent pathways. On the other
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decreased the expression of BCL2. This was in agreement with previous studies, which showed
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35 that oxaliplatin induced p53-mediated cycle arrest and (to a smaller degree) p53-mediated
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affect RAS cytotoxicities compared to OXP. This further confirmed that the RAS complexes
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42 acted via a p53-independent mode-of-action.
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45 To ascertain that the p53-independent activity is a general characteristic of this class of
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iminoquinoline-containing RAS complexes, we measured p53 expression following 24 h
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50 treatment at IC concentrations for the remaining complexes 1, 2, 3, 6 and 7 as well as measured
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viabilities of treated cells after 48 h in the absence and presence of pifithrin-α. Likewise, OXP
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was used as a positive control. There was a lack of p53 induction by these RAS complexes and
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lower cell viabilities in cells co-treated with pifithrin-α (Fig S3), in keeping with the other RAS
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complexes.
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9 In general, all RAS complexes tested in this studies demonstrated p53-independent activity,
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even though their physicochemical properties such as stability to nucleophiles and
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hydrophobicity differed significantly. A similar class of Ru (II) arene complexes bearing imino-
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16 and azo-pyridine ligands (Fig 1; top-right) has been shown to demonstrate p53-independent
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choice of halide ligand strongly influenced the p53-dependence on their class of compound. The
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23 key difference with RAS complexes was that they demonstrated p53-independent activities
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without the need for iodide substitution. The iminoquinoline and Ru (II)-arene functionalities
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28 common to all 9 RAS complexes were crucial for the observed p53-independence cytotoxicity
29
30 and structural tuning at the non-halide sites could be used to fine-tune their antiproliferative
31
32
modes-of action.
33
34
35
36 CONCLUSION
37
38
39 The current study gives insights to the structural determinants of cytotoxicity and p53-
40
41
independence in Ru (II)-arene complexes through a detailed chemical and in vitro SAR study of
42
43
44 9 RAS complexes. In general, the more hydrophobic complexes displayed higher cellular
45
46 accumulation and cytotoxicity across a panel of cancer cell lines. In addition, the lack of OCT
47
48
involvement in the uptake of RAS complexes suggested that entry occurred mainly via passive
49
50
51 diffusion, despite the fact that these complexes were hydrophilic in nature. RAS complexes also
52
53 displayed tolerance towards aquation, although analogues with benzene or toluene ligands were
54
55
significantly less stable towards biological nucleophiles as these arenes were much more prone
56
57
58
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to displacement. These complexes also exerted their anticancer activities via p53-independent
4
5
pathways as seen in the lack of activation of p53 and downstream targets, and their unchanged
6
7
8 activity in the presence of small molecule p53-inhibitors. Compounds such as this may have
9
10
important implication in the treatment of resistant cancers with mutated p53 or p53-null status.
11
12
13
14
15
16
17 EXPERIMENTAL
18
19
20 Materials. All experimental procedures were carried out without additional precautions to
21
22
exclude air or moisture unless otherwise specified. All chemicals and solvents were used as
23
24
25 received unless otherwise specified. Dry ethanol and methanol were obtained by drying them
26
27 over molecular sieves 3-4 Å 24 h before use. RuCl .xH O was purchased from both Precious
3 2
28
29
30 Metals Online. [(η6-benzene)RuCl ] , [(η6-toluene)RuCl ] , [(η6-cymene)RuCl ] , [(η6-
2 2 2 2 2 2
31
32 hexamethylbenzene)RuCl ] and [(η6-1,3,5-triisopropylbenzene)RuCl ] were synthesized
2 2 2 2
33
34
according to previously reported protocols.43, 54-56 Thiazolyl blue tetrazolium bromide (MTT),
35
36
37 Trizma® Base BioUltra, Nonidet P-40, DL-Dithiothreitol, Non-fat Dried Milk Bovine,
38
39
TWEEN® 20, Ponceau S and Cimetidine, were purchased from Sigma-Aldrich. All other
40
41
chemicals used were purchased from Sigma-Aldrich (Singapore). Ultrapure water used was
42
43
44 purified by a Milli-Q UV purification system (Sartorius Stedim Biotech SA). Gibco® Versene
45
46
solution, Gibco® Trypsin/EDTA solution, 10% SDS solution, Penicillin-Streptomycin (10 000
47
48
49 U/mL), Dulbecco's Phosphate-Buffered Saline (10x), TRIzol® Reagent and Applied
50
51 Biosystem® High Capacity cDNA Reverse Transcription Kit were purchased from Life
52
53
Technologies. HycloneTM RPMI 1640, DMEM medium and Fetal bovine serum (FBS) was
54
55
56 purchased from Thermo Fisher Scientific Inc. Bio-rad Protein Assay Dye Reagent Concentrate,
57
58
59
60
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40% Acrylamide/Bis solution, 10x Tris/glycine buffer, TEMED, 4x Laemmli Sample Buffer,
4
5
Nitrocellulose Membrane, 0.2 µm and 0.45 µm were purchased from Bio-rad Laboratories.
6
7
8 cOmplete, mini Protease Inhibitor Cocktail Tablets, RNase A, FastStart Universal Probe Master
9
10 (Rox) were purchased from Roche Diagnostics. LuminataTM Classico Crescendo Western HRP
11
12
13 Substrate were purchased from Merck Millipore Corporation.
14
15
16 Instrumentation. 1H NMR spectrums were obtained using either a Bruker AMX 300, Avance
17
18
400 or AMX 500 spectrometer and the chemical shifts (δ) were reported in parts per million with
19
20
reference to residual solvent peaks. Electrospray-ionization Mass Spectrometry (ESI-MS) spectra
21
22
23 were obtained using Thermo Finnigan MAT ESI-MS System. UV-vis spectra were obtained
24
25
using the Shimadzu UV-1800 UV Spectrophotometer with a TCC-240A Temperate Controlled
26
27
28 Cell Holder. Ru concentrations were determined using the Optima ICP-OES (Perkin-Elmer)
29
30 operated by CMMAC, NUS. Elemental analyses of selected Ru complexes were carried out
31
32
using a Perkin-Elmer PE 2400 elemental analyzer by CMMAS, NUS.
33
34
35
36 HPLC analysis of compound purity. Determination of the purity of the RAS Complexes were
37
38 done using analytical HPLC on a Shimadzu Prominence System equipped with a DGU-20A
3
39
40
Degasser, two LC-20AD Liquid Chromatography Pump, a SPD-20A UV/Vis Detector and a
41
42
43 Shim Pack GVP-ODS 2.0 mm 18 column (5 µM, 120Å, 250 mm x 4.60 mm i.d.) at r.t. at a flow
44
45 rate of 1.0 mL/min with detection at both 214 nm and 254 nm. The gradient elution conditions
46
47
were as follows: 20-80% solvent B over 30 min, where solvent A is 10 mM NH OAc pH 7.0 and
48 4
49
50 solvent B is CH CN.
3
51
52
53 Synthesis of 1, [(η 6 -benzene)RuCl(4-methoxy-N-(2-quinolinylmethylene)-aniline)]Cl. 2-
54
55
Quinolinecarboxaldehyde (78.6 mg, 0.5 mmol) and p-anisidine (61.5 mg, 0.5 mmol) was added
56
57
58
59
60
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to dry EtOH (10 mL) and and stirred at r.t. over 24 h. The solvent was removed in vacuo and
4
5
dried. The resultant crude 4-methoxy-N-(2-quinolinylmethylene)-aniline (94 mg, approx. 0.36
6
7
8 mmol) was treated with [(η6-benzene)RuCl ] (89.6 mg, 0.18 mmol) in MeOH (20 mL) and
2 2
9
10
stirred at r.t. over 12 h. The solvent was removed in vacuo and the resulting solid purified by
11
12
13 gradient elution column chromatography (1:1 v/v EtOH/CHCl 3 , R f = 0.2; EtOH, R f = 0.5). The
14
15 purified product was redissolved in CHCl and filtered through a syringe column to remove trace
3
16
17
amount of dissolved silica, before the solvent was removed in vacuo. The final product was then
18
19
20 dried in vacuo for 1 h to give a dark red solid. Yield: 40 mg (22%). 1H NMR (400 MHz, D O): δ
2
21
22 8.68 (d, 3J= 9 Hz, 1H, quinolinyl), 8.57 (s, 1H, PhN=CH), 8.35 (d, 3J = 8 Hz, 1H, quinolinyl),
HH
23
24
8.07 (t, 3J = 8 Hz, 1H, quinolinyl), 8.01 (d, 3J = 8 Hz, 1H, quinolinyl), 7.87 (t, 3J = 8 Hz,
25 HH HH HH
26
27 1H, quinolinyl), 7.81 (d, 3J = 8 Hz, 1H, quinolinyl), 7.74 (d, 3J = 9 Hz, 2H, C H OMe), 7.05
HH HH 6 4
28
29 (d, 3J = 9 Hz, 2H, C H OMe), 5.83 (s, 6H, C H ), 3.88 (s, 3H, OCH ) ppm. ESI-MS (+ve
30 HH 6 4 6 6 3
31
mode): m/z = 477 [M]+. ). Purity of the complex was determined to be >95% pure by RP-HPLC
32
33
34 (% Purity): 95.8% at 214 nm and 96.4% at 254 nm; t = 12.5 min.
r
35
36
37 Synthesis of 2, [(η 6 -toluene)RuCl(4-methoxy-N-(2-quinolinylmethylene)-aniline)]Cl. 2 was
38
39
obtained with [(η6-toluene)RuCl ] (94.6 mg, 0.18 mmol) and crude 4-methoxy-N-(2-
40 2 2
41
42 quinolinylmethylene)-aniline (94 mg, approx. 0.36 mmol) using the same protocol as used for 1
43
44
(Gradient elution: 1:4 v/v EtOH/CHCl , R = 0.2; EtOH, R = 0.7). The final product was then
45 3 f f
46
47 dried in vacuo for 1 h to give a dark red solid. Yield: 65 mg (35%). 1H NMR (400 MHz, DMSO-
48
49 d6): δ 9.16 (s, 1H, PhN=CH), 8.89 (d, 3J = 8 Hz, 1H, quinolinyl), 8.76 (d, 3J = 9 Hz, 1H,
HH HH
50
51
quinolinyl), 8.31 (t, 3J = 8 Hz, 2H, quinolinyl), 8.15 (t, 3J = 7 Hz, 1H, quinolinyl), 7.99 (m,
52 HH HH
53
54 3H, quinolinyl /C H OMe), 7.22 (d, 3J = 9 Hz, 2H, C H OMe), 6.07 (t, 3J = 6 Hz, 1H,
6 4 HH 6 4 HH
55
56 C H ), 6.01 (d, 3J = 6 Hz, 1H, C H ), 5.81 (t, 3J = 6 Hz, 1H, C H ), 5.71 (t, 3J = 6 Hz, 1H,
6 5 HH 6 5 HH 6 5 HH
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3 C H ), 5.37 (d, 3J = 6 Hz, 1H, C H ), 3.90 (s, 3H, ArOCH ), 2.17 (s, 3H, CH ) ppm. ESI-MS
6 5 HH 6 5 3 3
4
5
(+ve mode): m/z = 491 [M]+. Purity of the complex was determined to be >95% pure by RP-
6
7
8 HPLC (% Purity): 98.1% at 214 nm and 95.8% at 254 nm; t = 14.4 min.
r
9
10
11 Synthesis of 3, [(η 6 -cymene)RuCl(4-methoxy-N-(2-quinolinylmethylene)-aniline)]Cl. 3 was
12
13
obtained with [(η6-cymene)RuCl ] (109.72 mg, 0.179 mmol) and crude 4-methoxy-N-(2-
14 2 2
15
16 quinolinylmethylene)-aniline (94 mg, approx. 0.358 mmol) using the same protocol as used for 1
17
18
(Gradient elution: 1:4 v/v EtOH/CHCl , R = 0.3; 1:1 v/v EtOH/CHCl , R = 0.5). The final
19 3 f 3 f
20
product was then dried in vacuo for 1 h to give a dark orange solid. Yield: 125 mg (61%). 1H
21
22
23 NMR (400 MHz, DMSO-d6): δ 9.15 (s, 1H, PhN=CH), 8.91 (d, 3J = 8 Hz, 1H, quinolinyl),
HH
24
25
8.73 (d, 3J = 9 Hz, 1H, quinolinyl), 8.32 (t, 3J = 7 Hz, 2H, quinolinyl), 8.17 (t, 3J = 7 Hz,
26 HH HH HH
27
28 1H, quinolinyl), 8.01 (t, 3J HH = 7 Hz, 1H, quinolinyl), 7.96 (d, 3J HH = 9 Hz, 2H, C 6 H 4 OMe), 7.23
29
30 (d, 3J = 9 Hz, 2H, C H OMe), 6.11 (d, 3J = 6 Hz, 1H, i-PrC H Me), 5.89 (d, 3J = 6 Hz, 1H,
HH 6 4 HH 6 4 HH
31
32
i-PrC H Me), 5.75 (d, 3J = 6 Hz, 1H, C H ), 5.39 (d, 3J = 6 Hz, 1H, C H ), 3.91 (s, 3H,
33 6 4 HH 6 4 HH 6 4
34
35 ArOCH ), 2.32 (sept, 1H, 3J = 7 Hz, CH(Me) ), 2.24 (s, 3H, i-PrArCH ), 0.90 (d, 3J = 7 Hz,
3 HH 2 3 HH
36
37 3H, CH(CH ) ), 0.74 (d, 3J = 7 Hz, 3H, CH(CH ) ) ppm. ESI-MS (+ve mode): m/z = 533
3 2 HH 3 2
38
39
[M]+. Purity of the complex was determined to be >95% pure by RP-HPLC (% Purity): 99.4% at
40
41
42 214 nm and 96.0% at 254 nm; t = 19.0 min.
r
43
44
45 Synthesis of 4, [(η 6 -hexamethylbenzene)RuCl(4-methoxy-N-(2-quinolinylmethylene)-
46
47
aniline)]Cl. Complex 4 was synthesized according to published procedure.35
48
49
50
51 Synthesis of 5, [(η 6 -1,3,5-triisopropybenzene)RuCl(4-methoxy-N-(2-quinolinylmethylene)-
52
53 aniline)]Cl. Complex 5 was synthesized according to published procedure.34
54
55
56
57
58
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3 Synthesis of 6, [(η 6 -1,3,5-triisopropybenzene)RuCl(N-(2-quinolinylmethylene)-1-naphthyl-
4
5
amine)]Cl. 2-Quinolinecarboxaldehyde (78.6 mg, 0.5 mmol) and 1-napthylamine (53.2 mg, 0.5
6
7
8 mmol) was added to dry EtOH (10 mL) and and stirred at r.t. over 24 h. The solvent was
9
10
removed in vacuo and dried. The resultant crude N-(2-quinolinylmethylene)-1-naphthylamine
11
12
13 (141 mg, approx. 0.5 mmol) was treated with [(η6-1,3,5-triisopropylbenzene)RuCl 2 ] 2 (188 mg,
14
15 0.25 mmol) in MeOH (20 mL) and stirred at r.t. over 12 h. The solvent was removed in vacuo
16
17
and the resulting solid purified by column chromatography (1:4 v/v EtOH/CHCl , R = 0.6). The
18 3 f
19
20 purified product was redissolved in CHCl and filtered through a syringe column to remove trace
3
21
22 amount of dissolved silica, before the solvent was removed in vacuo. The final product was then
23
24
dried in vacuo for 1 h to give a dark red solid. Yield: 198 mg (62%). 1H NMR (400 MHz,
25
26
27 CD OD): δ 9.12 (s, 1H, PhN=CH), 8.91 (d, 3J = 12 Hz, 1H, quinolinyl), 8.86 (d, 3J = 11 Hz,
3 HH HH
28
29
1H, quinolinyl), 8.18 (m, 8H, quinolinyl/napthyl), 7.72 (m, 3H, quinolinyl/napthyl), 5.86 (s, 3H,
30
31
C H ), 2.18 (sept, 3J = 9 Hz, 3H, CHMe ), 1.07 (d, 3J = 9 Hz, 9H, CH(CH ) ), 0.98 (d, 3J
32 6 3 HH 2 HH 3 2 HH
33
34 = 9 Hz, 9H, CH(CH ) ) ppm. ESI-MS (+ve mode): m/z = 623 [M]+. Purity of the complex was
3 2
35
36
determined to be >95% pure by elemental analysis. Anal. Calcd for C H Cl N Ru·H O (%): C
37 35 38 2 2 2
38
39 62.12, H 5.96, N 4.14; Found: C 62.29, H 5.59, N 4.18.
40
41
42 Synthesis of 7, [(η 6 -1,3,5-triisopropybenzene)RuCl(3-trifluoromethyl-N-(2-quinolinyl-
43
44
methylene)aniline)]Cl. 2-Quinolinecarboxaldehyde (78.6 mg, 0.5 mmol) and 3-
45
46
47 (trifluoromethyl)aniline (62.5 µl, 0.5 mmol) was added to dry EtOH (10 mL) and and stirred at
48
49 r.t. over 24 h. The solvent was removed in vacuo and dried. The resultant crude 3-
50
51
trifluoromethyl-N-(2-quinolinylmethylene)aniline (150 mg, approx. 0.5 mmol) was treated with
52
53
54 [(η6-1,3,5-triisopropylbenzene)RuCl ] (188 mg, 0.25 mmol) in MeOH (20 mL) and stirred at r.t.
2 2
55
56 over 12 h. The solvent was removed in vacuo and the resulting solid purified by gradient elution
57
58
59
60
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column chromatography (1:4 v/v EtOH/CHCl , R = 0.4; 1:1 v/v EtOH/CHCl , R = 0.7). The
3 f 3 f
4
5
purified product was redissolved in CHCl and filtered through a syringe column to remove trace
6 3
7
8 amount of dissolved silica, before the solvent was removed in vacuo. The final product was then
9
10 dried in vacuo for 1 h to give a light brown solid. Yield: 156 mg (46%). 1H NMR (400 MHz,
11
12
13 DMSO-d6): δ 9.23 (s, 1H, PhN=CH), 8.96 (d, 3J HH = 9 Hz, 1H, quinolinyl), 8.91 (d, 3J HH = 8 Hz,
14
15 1H, quinolinyl), 8.53 (s(broad), 1H, C H ), 8.43 (d, 3J = 8 Hz, 1H, C H ), 8.31 (t, 3J = 8 Hz,
6 4 HH 6 4 HH
16
17
2H, quinolinyl), 8.16 (t, 3J = 9 Hz, 1H, quinolinyl/C H ), 8.01 (t, 3J = 8 Hz, 2H,
18 HH 6 4 HH
19
20 quinolinyl/C H ), 7.91 (t, 3J = 8 Hz, 1H, quinolinyl/C H ), 5.60 (s, 3H, C H ), 2.37 (sept, 3J
6 4 HH 6 4 6 3 HH
21
22 = 7 Hz, 3H, CHMe ), 1.16 (d, 3J = 7 Hz, 9H, CH(CH ) ), 0.84 (d, 3J = 7 Hz, 9H, CH(CH ) )
2 HH 3 2 HH 3 2
23
24
ppm. ESI-MS (+ve mode): m/z = 641 [M]+. Purity of the complex was determined to be >95%
25
26
27 pure by elemental analysis. Anal. Calcd for C H Cl F N Ru·3H O (%): C 52.60, H 5.66, N
32 35 2 3 2 2
28
29
3.83; Found: C 52.43, H 5.46, N 3.84.
30
31
32 Synthesis of 8, [(η 6 -1,3,5-triisopropybenzene)RuCl(3-chloro-N-(2-quinolinylmethylene)-
33
34
35 aniline)]Cl. 2-Quinolinecarboxaldehyde (78.6 mg, 0.5 mmol) and 3-chloroaniline (52.9 mg, 0.5
36
37
mmol) was added to dry EtOH (10 mL) and stirred at r.t. over 24 h. The solvent was removed in
38
39
vacuo and dried. The resultant crude 3-chloro-N-(2-quinolinylmethylene)aniline (133 mg,
40
41
42 approx. 0.5 mmol) was treated with [(η6-1,3,5-triisopropylbenzene)RuCl ] (188 mg, 0.25 mmol)
2 2
43
44
in MeOH (20 mL) and stirred at r.t. over 12 h. The solvent was removed in vacuo and the
45
46
47 resulting solid purified by column chromatography (1:4 v/v EtOH/CHCl 3 , R f = 0.6). The purified
48
49 product was redissolved in CHCl and filtered through a syringe column to remove trace amount
3
50
51
of dissolved silica, before the solvent was removed in vacuo. The final product was then dried in
52
53
54 vacuo for 1 h to give a dark red solid. Yield: 89 mg (28%). 1H NMR (400 MHz, MeOD-d4): δ
55
56 9.02 (d, 3J = 9 Hz, 1H, quinolinyl), 9.00 (s, 1H, PhN=CH), 8.79 (d, 3J = 8 Hz, 1H,
HH HH
57
58
59
60
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3 quinolinyl), 8.25 (m, 3H, quinolinyl/C H ), 8.15 (t, 3J = 8 Hz, 1H, quinolinyl/C H ), 8.06 (dt,
6 4 HH 6 4
4
5
3J = 5 Hz, 1H, quinolinyl/C H ), 7.99 (t, 3J = 8 Hz, 1H, quinolinyl/C H ), 7.65 (d, 3J = 5
6 HH 6 4 HH 6 4 HH
7
8 Hz, 2H, quinolinyl/C H ), 5.60 (s, 3H, C H ), 2.49 (sept, 3J = 7 Hz, 3H, CHMe ), 1.23 (d, 3J
6 4 6 3 HH 2 HH
9
10 = 7 Hz, 9H, CH(CH ) ), 0.97 (d, 3J = 7 Hz, 9H, CH(CH ) ) ppm. ESI-MS (+ve mode): m/z =
11 3 2 HH 3 2
12
13 607 [M]+. Purity of the complex was determined to be >95% pure by elemental analysis. Anal.
14
15 Calcd for C H Cl N Ru·3H O (%): C 53.41, H 5.93, N 4.02; Found: C 53.02, H 5.66, N 3.87.
31 35 3 2 2
16
17
18 Synthesis of 9, [(η 6 -hexamethylbenzene)RuCl(3-chloro-N-(2-quinolinylmethylene)-
19
20
21 aniline)]Cl. Complex 9 was synthesized according to published procedure.34
22
23
24 Alternative synthetic route for 8 and 9. 2-Quinolinecarboxaldehyde (314 mg, 2 mmol) and 3-
25
26
chloroaniline (268 mg, 4 mmol) were placed to a 50 mL round-bottom flask equipped with a
27
28
Dean-Stark apparatus. 25 mL of toluene was added to dissolve the reactants and the resulting
29
30
31 brown solution was refluxed overnight. The mixture was allowed to cool and concentrated under
32
33
reduced pressure to give the dark brown oil which was dissolved in a minimal amount of diethyl
34
35
36 ether. The black insoluble residue was filtered and the solution was again concentrated under
37
38 reduced pressure and dried in vacuo to give a brown semi-solid. The crude product containing
39
40
small amount of unreacted 3-chloroaniline was used without additional purification. 1H NMR
41
42
43 (300 MHz, d6-DMSO): δ 8.79 (s, 1H, Ph-N=CH), 8.53 (d, J = 8.6 Hz, 1H, quinolinyl), 8.29 (d, J
44
45 = 8.6 Hz, 1H, quinolinyl), 8.12 (dd, J = 15.9, 7.9 Hz, 2H, quinolinyl), 7.90 – 7.83 (m, 1H,
46
47
quinolinyl), 7.76 – 7.69 (m, 1H, quinolinyl), 7.54 – 7.47 (m, 2H, quinolinyl), 7.43 – 7.35 (m, 2H,
48
49
50 quinolinyl). The corresponding [(η6-arene)RuCl ] (0.15 mmol) and 3-chloro-N-(2-
2 2
51
52
quinolinylmethylene)-aniline (180 mg, 0.675 mmol) were dissolved in 10 mL of dry MeOH
53
54
under N atmosphere and stirred for 48 h. A resulting brown solution was evaporated under
55 2
56
57 reduced pressure and the brown residue was washed with copious amounts of diethyl ether. The
58
59
60
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solid was subsequently dissolved in minimal amount of CH Cl and eluted through a short layer
2 2
4
5
of neutral Al O (5 cm) by CH Cl to remove unreacted 3-chloro-N-(2-
6 2 3 2 2
7
8 quinolinylmethylene)aniline and 3-chloroaniline. The product was eluted with CHCl /MeOH
3
9
10
mixture (9:1) and the red filtrate was evaporated to dryness under reduced pressure. The red solid
11
12
13 was redissolved in a minimal amount of dichloromethane and centrifuged (13,000 rpm for 7 min)
14
15 to remove the undissolved residues. The red microcrystals (8) or needle-shaped X-ray quality
16
17
single crystals (9) were produced by slow diffusion of diethyl ether into the CH Cl solutions.
18 2 2
19
20 Crystals were washed with diethyl ether and dried in vacuo.
21
22
23 Complex 8. Yield: 38 mg (20%). Anal. Calcd, C H Cl N Ru·0.25 CH Cl (%): C, 56.50; H,
31 35 3 2 2 2
24
25
5.39; N, 3.22. Found: C, 56.09; H, 5.04; N, 4.46.
26
27
28
Complex 9. Yield: 40 mg (22%). Anal. Calcd, C H Cl N Ru·2CH Cl ·0.25 H O (%): C, 50.45,
29 28 29 3 2 2 2 2
30
31 H, 4.60, N, 4.06. Found: C, 50.36, H, 5.01, N, 4.21.
32
33
34
Tissue culture. The human colorectal carcinoma cells HCT116, human colorectal
35
36
adenocarcinoma cells SW480, human gastric adenocarcinoma AGS, human gastric carcinoma
37
38
39 KATOIII were acquired from ATCC® (Manassa,VA). HCT116 and SW480 were cultured in
40
41
DMEM medium containing 10% FBS and 1% Penicillin/Steptomycin (complete DMEM). AGS
42
43
44 was cultured in RPMI 1640 medium containing 10% FBS and 1% Penicillin/Steptomycin.
45
46 KATOIII was cultured in RPMI 1640 medium containing 20% FBS and 1%
47
48
Penicillin/Steptomycin. All cell lines were grown at 37 °C in a humidified atmosphere of 95%
49
50
51 air and 5% CO . Experiments were performed on cells within 20 passages.
2
52
53
54 Determination of Log P . Log P of the RAS complexes were determined using the shake
ow ow
55
56
flask method.38 The RAS complex were predissolved in ddH O that was presaturated with n-
57 2
58
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octanol (for 24 h and left to stand until phase separation occurs). The UV-vis spectrum for each
4
5
samples was obtained and the absorbances at the λ of each compound were determined. Equal
6 max
7
8 volume of n-octanol was added to each sample solution and the heterogeneous mixtures shaked
9
10
for 2 h before centrifuging at 4000 rpm for 1 min to achieve phase separation. The final
11
12
13 absorbance of the aqueous phase at the λ max of each compound were determined and their water-
14
15 octanol partition coefficient were calculated. All experiments were done in triplicate.
16
17
18
Inhibition of cell viability assay. The anti-proliferation activity the RAS Complexes on
19
20
exponentially growing cancer cells were determined using MTT assay as described previously.57
21
22
23 HCT116, SW480, AGS and KATOIII were seeded at 10 000 cells per well (100 µL) in Cellstar®
24
25
96-well plates (Greiner Bio-One) and incubated for 24 h. Thereafter, cancer cells were exposed
26
27
28 to drugs at different concentration in media for 48 h. The final concentration of DMSO in
29
30 medium was < 1% (v/v) at which cell viability was not significantly inhibited. The medium was
31
32
removed and replaced with MTT solution (100 µL, 0.5 mg/mL) in media and incubated for an
33
34
35 additional 45 min. Subsequently, the medium was aspirated, and the purple formazan crystals
36
37
dissolved in DMSO (100 µL). The absorbance due to the dissolved purple formazan was then
38
39
obtained at 565 nm. Inhibition to cell viability was evaluated with reference to the IC value,
40 50
41
42 which is defined as the concentration needed for a 50% reduction of survival based on the
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survival curves. IC values were calculated from the dose - response curves (cell viability vs
45 50
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47 drug concentration) obtained in repeated experiments and adjusted to actual [Ru] administered,
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49 which was determined using ICP-OES. The experiments were performed in 4 replicates for each
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drug concentration and were carried out at least three times independently.
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For cell viability assays involving inhibitors, Cimetidine (1.5 mM) were added together with test
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57 compounds and incubated for 7 h. Thereafter, the drugs were removed and replace with fresh
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media for the remainder of the 48 h. Pilfithrin-α (10 µM) was incubated with drugs for the entire
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48 h duration. Cell viability in the absence and presence of inhibitor was normalized against
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8 untreated control. Experiments were performed in 3 replicates and carried out at least three times
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independently.
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Drug uptake studies. HCT116 cells were grown on Cellstar® 6-well plates (Greiner Bio-One)
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16 at a density of 500 000 cells/well for 24 h before being treated with complexes 1 – 5, 6 and
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oxaliplatin at 1.5 µM for 24 h. Thereafter, the drug-containing media was removed and washed
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once with EDTA/PBS followed by trypsinization. The cells were collected, counted and digested
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23 separately with 69% nitric acid. The samples were diluted to a final concentration of 2% nitric
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acid and the Ru or Pt content quantified via ICP-MS. Experiments were performed three times
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28 independently.
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31 Antibodies and Western blot protocol. HCT116 cells were grown on Cellstar® 6-well plates
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(Greiner Bio-One) at a density of 500 000 cells/well for 24 h before being treated with
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36 complexes 4, 5, 8 and 9 at IC 50 and IC 75 for 2 h, 6 h and 24 h. Oxaliplatin treatment at IC 50 and
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38 IC was used as a positive control for several experiments. The cells were lysed with lysis buffer
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[100 µL, 1% NP40, 150 mM NaCl, 50 mM Tris-HCl (pH 8.0), protease inhibitor]. The cell
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43 lysate were transferred to separate 2 mL tubes and sonicated for 10 s. The samples were then
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45 centrifuged at 13000 rpm, 4˚C for 15 min. The supernatant liquid containing the proteins were
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collected and total protein content of each sample was quantified via Bradford’s assay. 50 µg of
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50 proteins from each sample were reconstituted in loading buffer [5% DDT, 1x Protein Loading
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Dye] and heated at 95˚C for 5 min. The protein mixtures were resolved on a 10% SDS-PAGE gel
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by electrophoresis and transferred to a nitrocellulose membrane. The proteins bands were
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57 visualized via enhanced chemiluminescence imaging (PXi, Syngene) after treatment with the
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primary antibodies and the appropriate secondary antibodies. Equal loading of protein was
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confirmed by comparison with actin. The following antibodies were used: p53 (FL-393), p21 (F-
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8 5) and Cyclin D1 (H-295) from Santa Cruz Biotechnologies. β-Actin (ab75186) from Abcam.
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ECL Anti-rabbit IgG (NA934V) and ECL Anti-mouse IgG (NA931) from GE Healthcare Life
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13 Sciences. All antibodies were used at 1:1000 dilutions except for actin (1:10000), anti-mouse and
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15 anti-rabbit (1:5000).
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Primers and qPCR protocol. Treatment conditions for HCT116 cells were similar to the
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protocol in western blot. RNA was extracted using TRIzol® Reagent and reverse transcription
21
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23 was performed with 2 µg of the extracted RNA using Applied Biosystem® High Capacity cDNA
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Reverse Transcription Kit with an Applied Biosystem® 2720 Thermal Cycler. Quantitative PCR
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28 was done on the resulting cDNA using FastStart Universal Probe Master (Rox) with Applied
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30 Biosystem® 7500 Real Time PCR System. The relative starting quantities of genes of interest
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32
were normalized against the housekeeping genes TBP and samples were done in duplicates. The
33
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35 specificity of the amplification was controlled by a melting curve. The gene and Assay ID of
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TaqMan probes are as follows: NOXA (Hs00560402_m1), BAX (Hs00180269_m1), BCL2
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39
(Hs00608023_m1) and TBP (Hs00427620_m1).
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45
ACKNOWLEDGEMENTS
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The authors thank staff of CMMAC, NUS for performing elemental analysis and ICP-OES
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51 analysis. They also thank Ligue contre le cancer, CNRS, European COST action CM1105,
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53 Ministry of Education and the National University of Singapore (R143-000-638-112) for funding
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the research presented in this study.
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