Structural Insights and Molecular Docking of Tyrosine Phosphatase (LTP-1) for Novel Anti-Periodontal Peptides Targeting Porphyromonas gingivalis.

Abstract

Periodontal diseases are chronic inflammatory conditions primarily driven by pathogenic bacteria such as Porphyromonas gingivalis, a keystone pathogen implicated in tissue destruction and immune dysregulation. Targeting bacterial virulence factors, particularly enzymatic regulators such as tyrosine phosphatases, offers a promising therapeutic strategy. Low molecular weight tyrosine phosphatase (LTP-1) plays a critical role in bacterial signaling, adhesion, and pathogenicity. The present study aimed to investigate the structural characteristics of LTP-1 and evaluate potential antimicrobial peptides (AMPs) targeting this protein through molecular docking approaches. The three-dimensional structure of LTP-1 was retrieved and refined using established protein databases. Candidate antimicrobial peptides were selected from curated peptide repositories based on their reported antibacterial activity. Molecular docking was performed using ClusPro to predict binding affinities and interaction profiles. The docking results demonstrated that selected peptides exhibited strong binding affinity toward the catalytic pocket of LTP-1, forming stable hydrogen bonds and hydrophobic interactions. Energy scoring revealed favorable binding energies ranging from −6.5 to −10.2 kcal/mol. These findings highlight the potential of peptide-based inhibitors targeting LTP-1 in P. gingivalis as a novel therapeutic approach for periodontal disease management. Further in vitro and in vivo validation studies are warranted to translate these findings into clinical applications..