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  • 02월 22일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Production of a Recombinant Antibacterial Peptide from the Bovine Lactophorin for Solid-state NMR Structural Study

등록일
2008년 2월 14일 12시 38분 12초
접수번호
1362
발표코드
29P86포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 <발표Ⅴ>
발표형식
포스터
발표분야
물리화학
저자 및
공동저자
박태준, 김용애
한국외국어대학교 화학과,
Component-3 of proteose peptone (PP3), also called lactophorin, is a minor phosphoglycoprotein found in bovine milk. Carboxyterminal 113 to 135 region of lactophorin is composed of a cationic amphipathic peptide which refers to as lactophoricin. Lactophoricin, 23-mer peptide, have been reported that they have an antimicrobial activity, but 17-mer peptide corresponding to the 119 to 135 region of lactophorin does not display an antimicrobial activity any more. In fact, it was interestingly known that the 17-mer and 23-mer peptides both interact with phospholipids, but only the 23-mer peptide can incorporate into planar lipidic bilayers by forming voltage-dependent channels. In order to understand the structure-activity relationship of these peptides, we cloned and expressed two recombinant peptides. Purification of lactophoricin was achieved by preparative reverse phased high performance liquid chromatography that yielded several milligram amounts of peptides. Integrity of the peptide was confirmed by NMR spectroscopy in the membrane-like environments.

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