Abstract
The exploration of antimicrobial peptides, such as thymosin β peptides, is crucial to reduce antibiotic dependence. Thymosin β peptides play roles in inflammation regulation, wound healing, cell migration, and angiogenesis, with recent attention on their antimicrobial potential. This study focuses on thymosin beta 3 peptide (Pmthymosin3) from Penaeus monodon, a 128 amino acid peptide identified through TA cloning of three gene isoforms. In silico analysis explored its antimicrobial properties and expression across tissues and developmental stages. Results show the highest expression in haemolymph, moderate in gills, and negligible in muscle. Developmental stage expression follows a concave-up pattern. Structural analysis reveals an α-helical configuration with scattered coils. Functional analysis highlights antimicrobial properties of Pmthymosin3, suggesting its potential applications in cancer treatment and biofilm mitigation. The physicochemical properties, combined with in silico findings, underscore Pmthymosin3 as a promising candidate for further antimicrobial research.
Published Version
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