Unveiling Encrypted Antimicrobial Peptides from Cephalopods' Salivary Glands: A Proteolysis-Driven Virtual Approach

• Type: Article in International Scientific Journal
• Date: 2024

Authors

Agüero-Chapin, G (Author) Other; Domínguez-Pérez, D (Author) Other; Marrero-Ponce, Y (Author) Other; Castillo-Mendieta, K (Author) Other; Agostinho Antunes (Author) FCUP

Journal

Title: ACS Omega

Vol. 9 No. 6

Publisher: American Chemical Society

Indexing

ISI Web of Knowledge - 1 Citation

Other information

Authenticus ID: P-017-9DM

DOI: 10.1021/acsomega.4c01959

Abstract (EN): Antimicrobial peptides (AMPs) have potential against antimicrobial resistance and serve as templates for novel therapeutic agents. While most AMP databases focus on terrestrial eukaryotes, marine cephalopods represent a promising yet underexplored source. This study reveals the putative reservoir of AMPs encrypted within the proteomes of cephalopod salivary glands via in silico proteolysis. A composite protein database comprising 5,412,039 canonical and noncanonical proteins from salivary apparatus of 14 cephalopod species was subjected to digestion by 5 proteases under three protocols, yielding over 9 million of nonredundant peptides. These peptides were effectively screened by a selection of 8 prediction and sequence comparative tools, including machine learning, deep learning, multiquery similarity-based models, and complex networks. The screening prioritized the antimicrobial activity while ensuring the absence of hemolytic and toxic properties, and structural uniqueness compared to known AMPs. Five relevant AMP datasets were released, ranging from a comprehensive collection of 542,485 AMPs to a refined dataset of 68,694 nonhemolytic and nontoxic AMPs. Further comparative analyses and application of network science principles helped identify 5466 unique and 808 representative nonhemolytic and nontoxic AMPs. These datasets, along with the selected mining tools, provide valuable resources for peptide drug developers.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 15