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Relationships between the Tertiary Structures and Biological Activities of Piscidin and Its Analogues Studied by NMR Spectroscopy

등록일
2005년 2월 17일 14시 40분 57초
접수번호
0928
발표코드
23P183포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
김유경, 함경수1, 김양미
건국대학교 화학과 구조화학연구실,
1조선대학교 생물신소재학과,
Piscidin 1 (Pis) is a cationic alpha-helical antibacterial peptide isolated from the mast cell of hybrid striped bass. Pis shows non-cell-selectivity with strong antibiotic activity against bacterial and mammalian cells. To design novel antibiotic peptides with bacterial cell selectivity, the effect of the mutation of two glycine residues (Gly8 and Gly13) on the structure, cell selectivity, interaction with model membranes and mode of antibiotic action were studied using NMR spectroscopy and fluorescence spectroscopy. Analogue peptide (Pis-PG) with a substitution of Gly8 with Proline shows bacterial cell selectivity. It has a bent structure near Gly8 and its N-terminal is buried deep into the SDS micelle. Pis-PG can be a potent candidate for new drug with high antibacterial activity without cytoxicity.

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