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학술발표회초록보기

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제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 The analysis of water network for kinase inhibitor potency and selectivity prediction: A case study of kinase binding to staurosporine

등록일
2014년 8월 28일 16시 19분 04초
접수번호
1218
발표코드
MEDI.P-973 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 15일 (수요일) 16:00~19:00
발표형식
포스터
발표분야
의약화학
저자 및
공동저자
장우대, 강남숙*
충남대학교 신약전문대학원, Korea
Protein kinases are of important drug target within the pharmaceutical industry. However, the design of potent and selective inhibitors can be challenging, because almost all protein kinases share the same fold and similar ATP binding sites. Here, in order to understand the kinase inhibitor potency and selectivity, we studied complexes of protein kinases with staurosporine. By molecular dynamics simulations, we investigated the structural role of water molecules. The hydrogen-bonded cyclic water rings within the ATP binding sites especially revealed significant features about the flexibility and the potential interactions of the protein kinases. Displacing water rings with frequent formation on the specific regions by kinase inhibitors has a propensity to enhance binding affinity. These results were compared to most current theoretical models that only consider steric and electrostatic factors. We found that desolvation effect is a critical role in protein-ligand binding mechanisms. This information can guide rational drug design by suggesting regions of the binding hot-spots that will be beneficial to displace by adding new chemical fragments to the ligand.

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