The repository administrator has not yet configured an RDF license.
The role of amino acid composition in the antibacterial activity of laterosporulin analogs
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 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.
HTML Summary of #3204 The role of amino acid composition in the antibacterial activity of laterosporulin analogs