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제112회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Mutation Effect on Amyloidogenic Human Protein β-2-microglobulin: Molecular Dynamics Simulations and Solvation Thermodynamics Analyses

등록일
2013년 8월 23일 19시 33분 10초
접수번호
0167
발표코드
PHYS.P-272 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 16일 (수요일) 16:00~19:00
발표형식
포스터
발표분야
물리화학
저자 및
공동저자
홍주연, 함시현*
숙명여자대학교 화학과, Korea
β2-microglobulin (β2-m) is a major component of amyloid fibrils deposited in patients suffering from dialysis-related amyloidosis. Recently, D76N and D59P mutants have been studied that are thermodynamically unstable and exhibit enhanced aggregation while W60C mutant is more stable and less prone to aggregate than wild-type. However, the structural and mechanistic features of different aggregation propensities of those mutants are still elusive. Here we carried out molecular dynamics simulations followed by solvation thermodynamics analyses to characterize the aggregation-prone structure of the wild type and its D76N, D59P, and W60C mutants. Compared to the native state structures determined by X-ray and NMR, the aggregation-prone structures are characterized by the exposure of the hydrophobic side-chains including proline cis-trans isomerization. Based on the solvation thermodynamic analysis, the aggregation-prone structures of D76N and D59P mutants exhibit greater hydrophobicity than those of wild-type and W60C mutant, which is in good agreement with the experimental observation. Understanding the structural and thermodynamic features of the aggregation-prone structures allow us to rationalize the experimentally observed higher aggregation propensity of the D76N and D59P mutants compared to the wild-type and W60C mutant.

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