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제122회 대한화학회 학술발표회, 총회 및 기기전시회 안내 The computational studies on the Binding Affinity properties of Stapled p53/HDM2 and Unstapled p53/HDM2 complexes

2018년 8월 30일 16시 22분 21초
PHYS.P-323 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 19일 (금요일) 11:00~12:30
Physical Chemistry
저자 및
Thi Diem Le, Haeri Im, Sihyun Ham*
Department of Chemistry, Sookmyung Women's University, Korea
The p53 tumor suppressor protein exerts antiproliferative effects, including growth arrest and apoptosis, in response to various types of stress pathways. In our body, p53 protein exists binding to HDM2 hence it will not active the tumor suppressor function. Therefore, the inhibition of p53/HDM2 interaction presents an appealing therapeutic strategy for the treatment of cancer. Previously, some developed structures have been constructed mimicking the epitope residues of p53 peptides and have been studied for their interaction with HDM2 proteins as well as hydrocarbon stapled peptides have found to make up a promising class of protein-protein interaction regulators. In this study, we report the structural and thermodynamic characteristics for the binding complex of the stapled p53/HDM2 and unstapled p53/HDM2. Moreover, we investigated the structural information of the complexes by molecular dynamics simulations. The binding free energy calculation based on the integral equation theory was also executed to quantify the binding affinity for the complex and to understand the factors of the binding affinity of the complexes. As a result, we found that the binding affinity of the stapled p53 peptide was higher than that for the corresponding unstapled peptide. We determined structurally and thermodynamically that the hydrocarbon linker contributes significantly to the high binding affinity of the stapled p53/HDM2.