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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Production and solid-state NMR structural studies of human Amyloid-β transmembrane peptide

등록일
2008년 8월 12일 11시 46분 46초
접수번호
1289
발표코드
33P230포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
박태준, 임수연, 김용애
한국외국어대학교 화학과, Korea
Recently, enormous progress has been made towards understanding of the cell biology and plaque properties of Alzheimer’s disease. But globular and nonfibrillar Amyloid-β proteins are continuously produced during normal cellular metabolism and are also present in Alzheimer tissues. In addition to it, small nonfibrillar Amyloid-β protein alone is sufficient to cause cellular degradation. One of the possible mechanisms for Amyloid-β protein toxicity suggests that nonfibrillar Amyloid-β protein form calcium-permeable ion channels in the cell plasma membrane. These channels might allow excessive calcium influx and disrupt the normal cellular calcium homeostasis. But little is known about the transmembrane region and the channel structure of Amyloid-β protein as an ion-channel protein as yet except theoretical model. We will elucidate the channel structure and mechanisms of their formation that is critical for developing therapeutic agents. Here, we report high-yield expression and purification of a transmembrane peptide comprising Aβ residues of the Amyloid -β protein. Initial structural data was obtained by solution NMR spectroscopy in the membrane-like environments. And we also present solid-state NMR structural studies of aligned samples of transmembrane peptide.

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