内在无序蛋白质
药物发现
计算生物学
化学生物学
小分子
折叠(DSP实现)
蛋白质折叠
生物
药品
结构生物学
药物靶点
化学
生物物理学
细胞生物学
生物化学
药理学
工程类
电气工程
标识
DOI:10.1016/j.cbpa.2010.06.169
摘要
Intrinsically disordered (ID) proteins that lack stable secondary and tertiary structure in substantial regions (or throughout) are prevalent in eukaryotes. They exist as ensembles of rapidly fluctuating structures and many undergo coupled folding and binding reactions. Because ID proteins are overrepresented in major disease pathways they are desirable targets for inhibition; however, the feasibility of targeting proteins without defined structures was unclear. Recently, small molecules have been found that bind to the disordered regions of c-Myc, Aβ, EWS-Fli1, and various peptides. As with structured targets, initial hits were further optimized to increase specificity and affinity. Given the number and biological importance of ID proteins, the ability to inhibit their interactions opens tremendous potential in chemical biology and drug discovery.
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