Integrative In Silico and Experimental Characterization of Endolysin LysPALS22: Structural Diversity, Ligand Binding Affinity, and Heterologous Expression.

ABSTRACT: Endolysins, phage-derived enzymes capable of lysing bacterial cell walls, hold significant promise as novel antimicrobials against resistant Gram-positive and Gram-negative pathogens. In this study, we undertook an integrative approach combining extensive in silico analyses and experimental validation to characterize the novel endolysin LysPALS22. Initially, sixteen endolysin sequences were selected based on documented lytic activity and enzymatic diversity, and subjected to multiple sequence alignment and phylogenetic analysis, which revealed highly conserved catalytic and binding domains, particularly localized to the N-terminal region, underscoring their functional importance. Building upon these sequence insights, we generated three-dimensional structural models using Swiss-Model, EBI-

SUBMITTER: Nawaz N 

PROVIDER: S-EPMC12429052 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature