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학술발표회초록보기

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  • 03월 02일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제117회 대한화학회 학술발표회, 총회 및 기기전시회 안내 NMR Structural Analysis of modified antimicrobial peptides with enhanced activities

등록일
2016년 2월 18일 15시 04분 04초
접수번호
3107
발표코드
ANAL2.O-14 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 10시 : 26분
발표형식
구두발표
발표분야
분석화학 - 젊은 분석화학자의 구두 발표 II (Oral Presentation of Young Analytical Chemists II)
저자 및
공동저자
김지선, 정지호, 김용애*
한국외국어대학교 화학과, Korea
Lactophoricin (LPcin), a cationic amphipathic peptide consists of 23-mer peptide, was currently utilized as the framework to design the novel analogs and study the effect of peptide hydrophobicity/hydrophilicity, amphipathicity on antimicrobial activities. LPcin analogs were designed and modified to enhance antibacterial activity using single/double amino acid substitutions, sequence shuffling for better amphipathic characteristics. Three candidates with enhanced antibacterial activity were selected among 12 LPcin analogs, the name of LPcin-YK1, LPcin-YK2 and LPcin-YK3 respectively. To understand the correlation between their structures and antibacterial mechanism, we studied how the modified conformation of LPcin analogs can affect their antimicrobial activity using bacterial killing and growth inhibition assays against Gram-negative and Gram-positive bacteria and antimicrobial activity of analogs showed to be higher than LPcin. A chemical and structural rationale for enhanced activity could be used as a guideline for design of novel antimicrobial peptides. We also successfully overexpressed LPcin analogs in the form of fusion protein in Escherichia coli and purified them from the cell extracts with many biophysical techniques. In order to investigate the structures, dynamics and 3D topology, we use various spectroscopic methods like MALDI-TOF MS and CD spectrometry, as well as 1D/2D solution NMR and solid-state NMR techniques in membrane environments. The structural calculations of LPcin analogs using Discovery Studio 2016 were also used to refine the orientational information of 3D structure and topology based on 2D SAMPI4 solid-state NMR spectra

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