[1P-2] ポスター1（1P-49ー1P-87）

[1P-86] IN SILICO DETERMINATION AND PEPTIDE ENGINEERING DEMONSTRATION OF POTENTIAL ANTIMICROBIAL PEPTIDES FROM COCOSIN-1

Nedrick T. Distor, ^○Anna Fatima M. Perea, Kuven A. Malig-on, Driyah Nicole E. Dario (Department of Biochemistry, College of Humanities and Sciences, De La Salle Medical and Health Sciences Institute)

The emergence of antimicrobial resistance prompted global efforts to significantly search and discover possible antibiotic substitutes such as antimicrobial peptides (AMPs) exhibiting an array of unique bioactivities. Utilizing cocosin-1, the major storage protein of Cocos nucifera L. as a possible source of AMPs, independent in silico enzymatic digestion (using pepsin, chymotrypsin, and trypsin) and AMP prediction yielded 9 AMPs (using CAMPR3) and 25 AMPs (using DeepAmPEP30). Peptide engineering of various combinations through amino acid (X) substitution of the top three cocosin-1 derived peptides revealed ¹²⁹QRSEREEGERHRW¹⁴¹ possessing the highest antimicrobial probability of about 82.45% when triple amino acid substitution (¹³⁰Arg to ¹³⁰X, ¹³⁶Gly to ¹³⁶X, ¹⁴¹Trp to ¹⁴¹X) was performed. Moreover, the peptide ³³QSPRRSVSSRNECRIERL⁵⁰ exhibited a 31.70% antimicrobial probability improvement when subjected to location-specific triple amino acid substitution. Results showed that distinct changes in the amino acid composition at specific positions may affect the antimicrobial probability of selected peptides. Further work should focus on the in vitro antimicrobial activity of the peptides and determine their unique microbicidal mechanisms.