Targeting the hydrophobic Phe43 pocket of HIV's envelope glycoprotein gp120 is a critical strategy for antiviral interventions due to its role in interacting with the host cell's CD4. Previous inhibit Show more
Targeting the hydrophobic Phe43 pocket of HIV's envelope glycoprotein gp120 is a critical strategy for antiviral interventions due to its role in interacting with the host cell's CD4. Previous inhibitors, including small molecules and CD4 mimetic peptides based on scyllatoxin, have demonstrated significant binding and neutralization capabilities but were often chemically synthesized or contained non-canonical amino acids. Microbial expression using natural amino acids offers advantages such as cost-effectiveness, scalability, and efficient production of fusion proteins. In this study, we enhanced the previous scyllatoxin-based synthetic peptide by substituting natural amino acids and successfully expressed it in E. coli. The peptide was optimized by mutating the C-terminal amidated valine to valine and glutamine, and by reducing the disulfide bonds from three to two. Circular dichroism confirmed proper secondary structure formation, and fluorescence polarization analysis revealed specific, concentration-dependent binding to HIV gp120, supported by molecular dynamics simulations. These findings indicate the potential for scalable microbial production of effective antiviral peptides, with significant applications in pharmaceutical development for HIV treatment. Show less
Abstract To assess the nature of the relationship between the integral conformational stability of tetrapeptides and the main types of β-turns (which are also tetrapeptides), spectrum diagrams, the as Show more
Abstract To assess the nature of the relationship between the integral conformational stability of tetrapeptides and the main types of β-turns (which are also tetrapeptides), spectrum diagrams, the asymmetry of the distribution of conformationally stable and unstable tetrapeptides have been calculated. It has been shown that β-turns of types I', II, and II' consist mainly of conformationally labile peptides; this is consistent with the context-predetermined nature of their structure. Since, as we have shown earlier, in this case the conformation is imposed by external conditions (specifically, the closure of the cycle), the prevalence of conformation-labile peptides facilitates the formation of the structure due to external factors. The type I β-turn is an exception, since peptides with different conformational lability are distributed fairly even in it. It can be assumed that the formation of the type I β-turn is not contextually determined. Show less
In the work the arguments are presented in favor of the idea on the role of conformationally stable oligopeptides in specific long-distance interactions in phenomena of molecular recognition during va Show more
In the work the arguments are presented in favor of the idea on the role of conformationally stable oligopeptides in specific long-distance interactions in phenomena of molecular recognition during various biological processes. Original authors’ and literature data are taken into account. The examples of conformationally stable short oligopeptides participating in alpha-helix and collagen type structures formation are given simultaneously with theoretical approaches. The conformationally stable oligopeptides obtained in the course of PDB bank analysis are discussed. The role of amino acid sequence in collagen helix formation is shown. Show less