Lytic Activity of Antimicrobial Peptides to Overcome Antibiotic Resistant Bacterial Threats
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Authors
Krinock, Matthew
Issue Date
2019-09-01
Type
Thesis
Language
en_US
Keywords
Alternative Title
Abstract
Antibiotic resistance is a growing global threat that researchers are trying to combat by exploring now possible solutions. Melittin (Mel) is an extensively studied antimicrobial peptide (AMP) that has significant antimicrobial properties. However, it has cytotoxic effects towards eukaryotic cells making its use limited. In this study, the lytic activity of four truncated Mel peptides (Mel-N18, Mel-C18, Mel-N22, Mel-C22) was analyzed to see if shortening the peptide would reduce the cytotoxic effects towards eukaryotic cells while maintaining antimicrobial properties. To analyze the potential of the four experimental peptides, several tests were conducted to generate bacterial growth curves used to determine their IC50s. Gram (-) E. coli and Gram (+) S. aureus, were subjected to treatments of each peptide at varying concentrations, demonstrating that Mel-N18 and Mel-C18 had minimal lytic activity in contrast with Mel-N22 and Mel-C22, which lysed both bacterial species at low concentrations. To analyze the cytotoxic effects of each peptide towards human eukaryotic cells, liposome lysis assays and human red blood cell (RBC) lysis assays were performed, which showed that only Mel-C22 was not cytotoxic to the liposomes and that only Mel-N22 was cytotoxic towards RBCs. Analysis of each test concluded that Mel-C22 is a promising candidate for further research due to a large reduction in cytotoxicity towards human eukaryotic cells and a maintenance of bacterial lytic activity.
Description
vi, 21 p.
Citation
Publisher
Kalamazoo College
License
U.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder. All rights reserved.