Selectivity Modulation of Antimicrobial Peptides to Enhance Pathogenic Targeting

Overview

As promising candidates for addressing pathogenic resistance, antimicrobial peptides (AMPs) are capable of lysing bacterial strains through membrane disruption, but many unintentionally penetrate non-target, healthy cells, implicating the potential cytotoxicity of AMPs. Due to the lack of known presence of cathelicidins in the human body, this study aimed to provide a novel approach, the co-modulation of bovine cathelicidin BMAP-27, to model pathways that increase potency against virulent bacterial strains. Eight analogs of BMAP-27 were created through amino acid substitutions that decreased hydrophobicity and increased cationic nature both distinctly and simultaneously in non-active and active regions of the peptide. Molecular docking of each analog and the bacterial membrane protein of interest resulted in the top docked structures being modeled to visualize the depth of penetration of the AMP analog and determine specific residues where high interactions occurred. Similar molecular docking simulations were conducted to model how each analog interacts with immune host cells. It was found that increasing the cationic nature distinctly and altering both factors simultaneously in BMAP-27 correlated with a stronger binding affinity and increased the stability of the binding complex concerning the pathogenic target. Additionally, statistical trends of successful peptide analogs established a 38% upper threshold for hydrophobicity and a +10 lower threshold for positive charge. These results suggest the potential for primary structure modifications to increase cathelicidins' capacity for selectively targeting pathogenic bacteria and, more broadly, the ability of such AMPs to be utilized in application to the human body without cytotoxic repercussions.

Competition history

• AJAS 2025 Category not listed

Related projects

Closest projects by meaning, across every fair and year in the corpus.

Browse more like this

• AJAS None projects
• Every AJAS 2025 project