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학술발표회초록보기

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제117회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structural and Thermodynamic Characteristics of the Strong Binding between cHLH and HDM2

등록일
2016년 2월 24일 22시 56분 04초
접수번호
1891
발표코드
PHYS.P-235 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
4월 21일 (목요일) 11:00~12:30
발표형식
포스터
발표분야
물리화학
저자 및
공동저자
임해리, 함시현*
숙명여자대학교 화학과, Korea
Tumor suppressor protein p53 loses its function upon binding with HDM2 protein, and inhibiting the p53-HDM2 interaction is critical to suppress tumor cell growth. Recently, the cyclized helix-loop-helix peptide (cHLH) mimicking the α-helix part of p53 protein has been designed and found to exhibit high binding affinity with HDM2. Here, we report the structural and thermodynamic characteristics for the binding complex of cHLH peptide with HDM2 protein. We performed molecular dynamics simulations to investigate the structural information of cHLH as well as its complex with HDM2. Also the binding free energy calculation based on the integral equation theory was executed to quantify the binding affinity for cHLH/HDM2 complex and to understand the factors to contribute binding affinity. We found the critical role of salt-bridge in the helix stability of cHLH as well as in the complexation with HDM2, which may provide an insight into the development of anti-cancer drug designs.

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