Publication:
PAPAIN-CATALYZED SYNTHESIS OF ALTERNATING ARGININE-TRYPTOPHAN PEPTIDES FOR ANTIMICRIOBIAL APPLICATIONS

dc.contributor.authorNichols, Kaleb
dc.contributor.authorEdson, Cody
dc.date.accessioned2026-04-22T19:29:14Z
dc.date.issued2026-04-16
dc.description.abstractAntimicrobial peptides represent a promising strategy for combating multidrug resistant pathogens. However, the conventional synthesis strategy using Solid Phase Peptide Synthesis (SPPS) relies on harsh reagents, extensive solvent use and costly, multi-step protocols. In this study, we investigate a greener and more efficient approach to synthesizing peptides using Protease-Catalyzed Peptide Synthesis (PCPS) to generate short arginine-tryptophan (Arg-Trp) peptides, molecules known to possess antimicrobial properties. We examine the enzymatic coupling of Arg-Trp dipeptides using papain, a well-documented protease, as a biocatalyst under mild conditions, promoting peptide bond formation through aminolysis rather than hydrolysis. The reaction products are characterized by MALDI-TOF mass spectrometry to assess peptide formation and composition. This approach aims to provide a cost-effective and environmentally sustainable alternative to traditional peptide synthesis, with findings that will inform future studies on alternative syntheses and antimicrobial efficacy of Arg–Trp peptides produced via PCPS.
dc.identifier.urihttps://dspace.husson.edu/handle/20.500.14298/1114
dc.language.isoen_US
dc.titlePAPAIN-CATALYZED SYNTHESIS OF ALTERNATING ARGININE-TRYPTOPHAN PEPTIDES FOR ANTIMICRIOBIAL APPLICATIONS
dc.typePoster
dspace.entity.typePublication
relation.isAuthorOfPublicationd3e89195-c9f5-4e19-926c-52273d4dbc4c
relation.isAuthorOfPublication.latestForDiscoveryd3e89195-c9f5-4e19-926c-52273d4dbc4c
Files
Original bundle
Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
2026-SH-16-poster.pdf
Size:
499.73 KB
Format:
Adobe Portable Document Format
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.45 KB
Format:
Item-specific license agreed to upon submission
Description: