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DFT study on the role of secondary structure propensity in oligomerization process of amyloid beta peptide

등록일
2008년 8월 11일 19시 02분 10초
접수번호
0777
발표코드
31P161포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
물리화학
저자 및
공동저자
홍주연, 함시현
숙명여자대학교 화학과, Korea
Alzheimer’s disease (AD), a neurodegenerative disorder, is a result of deposition in brain tissues of A peptides, a normal product in the amyloid precursor protein metabolism. It is known that polypeptide aggregation proceeds through the formation of transient intermediates which assemble into more stable oligomers which is characterized by a common cross β-sheet structure. But the aggregation mechanisms in the amyloid structures with a characteristic cross-β-pattern are still elusive part. Among Aβ1-42 sequences which are the major components of the plaques, 16-22 residues (KLVFFAE) are widely known as the central hydrophobic core to form oligomers or fibrils. Because the seven residues would be the significant region to form fibril, the (Ala)7 is employed to detect the secondary structure propensity on the Ramachandran plot. The DFT results of Alanine heptapeptide would present the preferences and the thermodynamic stability of secondary structures formations in the process of Aβ oligomerization.

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