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  • 09월 08일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제116회 대한화학회 학술발표회, 총회 및 기기전시회 안내 NMR Structural Analysis of Antimicrobial peptides, LPcin analogs, with Enhanced Activities in membrane environments [우수포스터상]

등록일
2015년 8월 27일 16시 23분 42초
접수번호
1001
발표코드
BIO.P-207 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 15일 (목요일) 11:00~12:30
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
정지호, 김지선, 김용애*
한국외국어대학교 화학과, Korea
Lactophoricin (LPcin), a cationic amphipathic peptide consists of 23-mer peptide, corresponds to the carboxy terminal 113?135 region of Component-3 of bovine proteose-peptone PP3. LPcin analogs were designed and modified to enhance antibacterial activity using mutation, shorten sequence, and sequence shuffling for better amphipathic characteristics. Three candidates with enhanced antibacterial activity were chosen among 12 LPcin analogs, the name of LPcin-YK1, LPcin-YK2 and LPcin-YK3 respectively, via agar hole diffusion test. 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 various biophysical techniques. We successfully overexpressed in the form of fusion protein in Escherichia coli and purified with several biophysical techniques. We performed MALDI-TOF MS and CD spectrometry for structure refinement. In order to investigate the structures and dynamics, we use various solution and solid state NMR techniques using the purified peptides with micelle and especially bicelle samples to mimic membrane environments. Finally we use structural calculations and MD simulation by using Discovery Studio 3.1 to compensate for solid state NMR data for structural refinement.

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