Peptide Libraries from Cephalopods' Posterior Salivary Glands for Potential Antimicrobial Peptides.

Published: 25 July 2023| Version 1 | DOI: 10.17632/6fjsdnvygb.1
Guillermin Agüero-Chapin, Dany Domínguez-Pérez, Yovani Marrero-Ponce


Filtered peptide libraries consisting of 11-40 amino acids (AA) were generated, comprising conventional AAs, and with intended use as a source of antimicrobial peptides (AMPs). These peptide libraries were constructed through various digestion protocols, including single enzyme applications (Trypsin, Chymotrypsin, Proteinase-K, AspN, and GluC), sequential mode with two enzymes (Tryp-Chym, Tryp-ProtK, Tryp-AspN, and Tryp-GluC), and concurrent mode with two enzymes (Tryp-Chym, Tryp-ProtK, Tryp-AspN, and Tryp-GluC). The peptide libraries were derived from the Composite Protein Database originating from Cephalopods' Posterior Salivary Glands.


Steps to reproduce

The 13 peptide libraries derived from 13 digestion protocols (DOI: 10.17632/c3zhzgwsnw.1) applied to the Composite Protein Database originating from the Cephalopods' Posterior Salivary Glands were processed as follows: - Peptides with lengths ranging from 6 to 40 amino acids (AAs) were selected. - Duplicated peptides within this length subset (6-40 AAs) were removed. - Peptide sequence redundancy was further eliminated by applying CD-HIT at 98% identity threshold, resulting in a peptide length range of 11-40 AAs. - Peptides of 11-40 AA length bearing conventional AAs were retained for analysis.


Universidade do Porto Centro Interdisciplinar de Investigacao Marinha e Ambiental


Biodiscovery, Omics, Peptide Library, Antimicrobial, Database