Antimicrobial peptides (AMPs) are integral components of the defense systems found in many organisms. To date, approximately 1500 AMPs have been characterized across a wide variety of species. The net positive charge of AMPs facilitates their selective interaction with negatively charged components of bacterial membranes, contributing to their antimicrobial specificity. In this study, we investigated the molecular design of AMPs derived from Cytobacillus firmus BWCVES08, an endophytic bacterium isolated from mangrove-associated plant species. The primary objective was to predict peptide-protein interactions using computational tools. The protein sequences were analyzed using EMBOSS and Expasy software. AMP prediction and structural analysis were conducted via the DBAASP database, and molecular docking was performed. This work aims to provide an in-silico framework for the design of novel AMPs for therapeutic application.