个人简介

1998-2005年分别以博士后、研究科学家、研究助理教授在美国托马斯杰弗逊大学、伊利诺大学、伯翰姆研究所学习和工作，期间设计出第一个Bcl-2小分子抑制剂-HA14-1，该抑制剂发表于PNAS并获一项美国专利。2005年入选中国科学院百人计划，受聘于上海药物研究所，任研究员、课题组长。

研究方向

采用生物化学、结构生物学方法，研究与癌症、神经退行性疾病相关蛋白质的结构与功能。

以这些蛋白质为靶标，设计全新化学结构的抑制剂或激动剂，为药物研发提供新的先导化合物。

发展蛋白质结构功能研究、药物分子设计的新方法和新技术。

专家类别

研究员；百人计划

职务

中科院上海药物所研究员、博士生导师、课题组长

代表论著

Zhou Y, Jiang C, Zhang Y, Liang Z, Liu W, Wang L, Luo C, Zhong T, Sun Y, Zhao L, Xie X, Jiang H, Zhou N, Liu D*, Liu H*. Structural Optimization and Biological Evaluation of Substituted Bisphenol A Derivatives as -Amyloid Peptide Aggregation Inhibitors. Journal of Medicinal Chemistry.

Feng Y, Ding X, Chen T, Chen L, Liu F, Jia X, Luo X, Shen X, Chen K, Jiang H, Wang H*, Liu H*, Liu D*. Design, Synthesis and Interaction Study of Quinazoline-2(1H)-Thione Derivatives as Novel Potential Bcl-xL Inhibitors. Journal of Medicinal Chemistry

Jiang C, Feng Y, Huang X, Xu Y, Zhang Y, Zhou N, Shen X, Chen K, Jiang H*, Liu D*. An enzyme-linked immunosorbent assay to compare the affinity of chemical compounds for -amyloid peptide as a monomer. Analytical and Bioanalytical Chemistry

Chen L, Feng Y, Zhou Y, Zhu W, Shen X, Chen K, Jiang H, Liu D*. Dual role of Zn2+ in maintaining structural integrity and suppressing deacetylase activity of SIRT1. Journal of Inorganic Biochemistry

Feng Y, Liu D*, Shen X, Chen K, Jiang H. Structure assembly of Bcl-xL through α5-α5 and α6-α6 interhelix interactions in lipid membranes. Biochimica et Biophysica Acta-Biomembranes

Feng Y, Wu J, Chen L, Luo C, Shen X, Chen K, Jiang H, Liu D*. A fluorometric assay of SIRT1 deacetylation activity through quantification of nicotinamide adenine dinucleotide. Analytical Biochemistry

Feng Y, Zhang L, Hu T, Shen X, Ding J, Chen K, Jiang H, Liu D*. A conserved hydrophobic core at Bcl-xL mediates its structural stability and binding affinity with BH3-domain peptide of pro-apoptotic protein. Archives of Biochemistry and Biophysics

Feng Y, Shen X, Chen K, Jiang H, Liu D*. A new assay based on fluorescence resonance energy transfer to determine the binding affinity of Bcl-xL inhibitors. Bioscience Biotechnology and Biochemistry