Generation of Peptide Libraries: Applying Various In silico Enzymatic Digestion Protocols on the Composite Protein Database (nr).

Published: 24 July 2023| Version 1 | DOI: 10.17632/c3zhzgwsnw.1
Contributors:
Guillermin Agüero-Chapin, Dany Domínguez-Pérez, Yovani Marrero-Ponce

Description

Peptide Diversity Generation through In silico Enzymatic Digestion of the Composite Protein Database (nr) from Cephalopod's Posterior Salivary Glands resulted in 13 distinct peptide libraries. These libraries were created using various digestion protocols, including just one enzyme (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).

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Steps to reproduce

1. The Composite Protein Database from Cephalopods' Posterior Salivary Glands underwent in silico enzymatic digestion using the Rapid Peptides Generator (RPG) tool (https://rapid-peptide-generator.readthedocs.io/en/latest/index.html). 2. Three enzymatic digestion protocols were employed: One Enzyme (Trypsin, Chymotrypsin, Proteinase-K, AspN, and GluC), Two Enzymes in Sequential mode (Tryp-Chym, Tryp-ProtK, Tryp-AspN, and Tryp-GluC), and Two Enzymes in Concurrent mode (Tryp-Chym, Tryp-ProtK, Tryp-AspN, and Tryp-GluC). This resulted in the generation of 13 distinct peptide libraries, with 5 libraries from the One Enzyme protocol and 4 libraries each from the Two Enzymes Sequential and Concurrent modes.

Categories

Biodiscovery, Omics, Peptide Library, Antimicrobial, Database

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