Targeting surface protein antigen I/II of Streptococcus mutans using novel WL10 antimicrobial peptide

Abstract

Background: Streptococcus mutans (S. mutans) is a leading cause of tooth decay because it sticks tightly to teeth and builds protective biofilms.
With rising antibiotic resistance making traditional treatments less effective, we urgently need new options. Antimicrobial peptides (AMPs) stand
out as promising solutions-they're targeted, low-risk, and highly effective against microbes. This study designed a new antimicrobial peptide
called WL10 and assessed its safety, bioavailability, and how it binds to S. mutans surface protein antigen I/II using computer-based methods.
Methods: WL10 was designed using specialized peptide design tools and visualized with the PepDraw server. Its toxicity was predicted using
ToxinPred, and bioavailability was assessed using Peptide Ranker. Physicochemical properties were analyzed using peptide property calculators.
Molecular docking simulations were performed using the HPEPDOCK server to evaluate the interaction between WL10 and the antigen I/II
protein, with binding affinity and stability assessed based on docking scores.
Results: ToxinPred confirmed WL10 is non-toxic. Peptide Ranker gave it a strong bioavailability score of 0.87, pointing to good biological
potential. Docking showed robust binding to the antigen I/II protein, with an affinity of −179 kcal/mol-evidence of a stable interaction that could
block the protein's function and disrupt bacterial adhesion.
Conclusion: Computational analyses indicate that the antimicrobial peptide WL10 is non-toxic, biologically active, and exhibits strong binding
affinity toward the key surface protein antigen I/II of S. mutans. These findings highlight its potential as a targeted anti-adhesive agent capable
of inhibiting bacterial colonization and biofilm formation. Further experimental validation, including in vitro and in vivo studies, is warranted to
confirm its therapeutic efficacy and clinical applicability.