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|
| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Event Hall |
| Time |
4월 20일 (금요일) 11:00~12:30 |
| Code |
BIO.P-309 |
| Subject |
Engineered antimicrobial peptides and their structural studies using NMR spectroscopy |
| Authors |
Ji Sun Kim, jiho jung, YONGAE KIM*
Department of Chemistry, Hankuk University of Foreign Studies, Korea
|
| Abstract |
Since wide spread of antibiotic resistance bacterial pathogens have been prevalent it is important to investigate new class of antimicrobial molecules, antimicrobial peptides (AMPs). Lactophoricin (LPcin), a cationic amphipathic peptide consists of 23-mer peptide from bovine milk, was currently utilized as the framework to design the novel analogs and study the correlation between structure-activity of AMPs. 11 LPcin analog peptides were designed to improve the antimicrobial activity, using conservative sequence modification and designed additional 9 analog peptides based on LPcin-YK3 which shows best antibacterial activity among them. Antimicrobial activity of designed novel AMPs was confirmed by bacterial killing assays and growth inhibition assays for Gram-negative and Gram-positive bacteria, and the stability was confirmed by hemolysis assay and cytotoxicity assay for eukaryotic cells. We conducted structural studies of analog peptides using various spectroscopic methods as well as NMR in order to clarify the correlation between antimicrobial activity and structure of AMPs. Analog peptides were obtained with high yield and high purity by optimizing expression using E. coli and purification using many biophysical techniques. Structures of analog peptides in membrane environments are studied using solid-state NMR to identify their 3D structures and topologies. |
| E-mail |
cucu860@daum.net |
|
121st General Meeting of the KCS