@article{open3204,
          volume = {136},
          number = {9},
           title = {The role of amino acid composition in the antibacterial activity of laterosporulin analogs},
          author = {Piyush Baindara and Vipul Solanki and Shelley Sardul Singh and Nayudu Nallabelli and Sumeeta Kumari and Pushpanjali Bhardwaj and Vishakha Grover and Krishan Gopal Thakur and Suresh Korpole},
            year = {2025},
           pages = {lxaf208},
         journal = {Journal of Applied Microbiology},
             url = {http://crdd.osdd.net/open/3204/},
        abstract = {This study aimed to compare the antimicrobial activity of the structural analogs of a class IId bacteriocin, laterosporulin.The antimicrobial peptide laterosporulin3 (LS3), produced by a Brevibacillus sp. strain SKR3, showed 96\% identity to earlier described laterosporulin (LS) and 60\% to laterosporulin10 (LS10) in amino acid composition. LS3 has a molecular weight of 5613{\^A} Da, the same as LS, yet differs in amino acid composition. Notable differences were found in their antimicrobial activity. Crystal structures of LS3 and LS10 were compared with LS. The analysis revealed that an additional Lys residue in LS3 enhances its net positive charge, leading to increased antimicrobial activity. FITC labeling showed the role of surface-displayed cationic Lys residues in the activity.Crystal structures of three different laterosporulins isolated from various strains of Brevibacillus were compared to understand the structure/function relationship. Results obtained in this study suggest that subtle variations in the amino acid composition of laterosporulins, distribution, and surface accessibility of charged residues can profoundly affect their antimicrobial activity.}
}