Publication: ALPHA-CHYMOTRYPSIN PROTEASE-CATALYZED PEPTIDE SYNTHESIS OF ALTERNATING ARGNINE-TRYPTOPHAN PEPTIDES AND THEIR ANTIMICROBIAL PROPERTIES
| dc.contributor.author | Lessa, Timothy | |
| dc.contributor.author | Edson, Cody | |
| dc.date.accessioned | 2026-04-22T19:32:16Z | |
| dc.date.issued | 2026-04-16 | |
| dc.description.abstract | Antimicrobial peptides (AMPs) are an increasingly popular topic in research due to their effectiveness against drug-resistant bacteria and pathogens. These peptides target the cell membrane of the bacteria and that makes them very difficult for bacteria to build resistance to. Due to this, AMPs are being developed to help treat viral infections, aid in wound healing, act as a safe preservative for agriculture, and could be used to target cancer cells. The conventional synthesis methods for antimicrobial peptides however often involve harsh chemicals, large amounts of waste, and high costs. Therefore, to investigate more environmentally and economically favorable synthesis strategies for AMPs we used an alternative synthesis method in Protease-Catalyzed Peptide Synthesis (PCPS). PCPS is conducted using water as a solvent and is relatively cheaper, uses less toxic reagents, and utilizes renewable protease enzymes as catalysts. We specifically sought to form a repeating Arginine-Tryptophan amino acid sequence because of tryptophan’s ability to anchor to a cell wall and arginine’s ability to destroy it, making them a great antimicrobial agent. The protease enzyme I chose to investigate this synthesis with is Alpha-Chymotrypsin, because while it favors the hydrolysis of Tryptophan-Arginine amide bonds, we can target the reverse aminolysis reaction by using Arginine-Tryptophan dipeptide units which interact with the active sight of the enzyme differently and favor aminolysis over hydrolysis. We predict that the Alpha-Chymotrypsin will yield a bell-curve like distribution of alternating peptide chains ranging from 2-16 amino acids in length, which is the typical range of amino acid chain length for PCPS reactions. We will also conduct an antimicrobial assay to determine the oligopeptide’s effectiveness against gram + and gram -bacteria and determine the minimum inhibition concentration. | |
| dc.identifier.uri | https://dspace.husson.edu/handle/20.500.14298/1115 | |
| dc.language.iso | en_US | |
| dc.title | ALPHA-CHYMOTRYPSIN PROTEASE-CATALYZED PEPTIDE SYNTHESIS OF ALTERNATING ARGNINE-TRYPTOPHAN PEPTIDES AND THEIR ANTIMICROBIAL PROPERTIES | |
| dc.type | Poster | |
| dspace.entity.type | Publication | |
| relation.isAuthorOfPublication | d3e89195-c9f5-4e19-926c-52273d4dbc4c | |
| relation.isAuthorOfPublication.latestForDiscovery | d3e89195-c9f5-4e19-926c-52273d4dbc4c |