化学
组织蛋白酶
生物活性
生物化学
二肽
酶
对接(动物)
活动站点
酶抑制剂
结构-活动关系
小分子
立体化学
拟肽
异羟肟酸
抑制性突触后电位
组织蛋白酶L
酶分析
组织蛋白酶D
分子模型
药物发现
虚拟筛选
组织蛋白酶A
体外
组织蛋白酶B
组织蛋白酶C
酶激活剂
组合化学
结合位点
作者
Marcin Kaźmierczak,Monika Bilska-Markowska,Katarzyna Wiśniewska,Małgorzata Pawełczak,Damian Nowak,Marcin Hoffmann
标识
DOI:10.1021/acs.joc.5c02923
摘要
)-α-fluorovinylphosphonates, with a key step involving the Horner-Wadsworth-Emmons (HWE) reaction. The synthesized compounds were evaluated as potential reversible inhibitors of the cathepsin C enzyme. Comprehensive characterization of the target molecules was performed, and their inhibitory activity was assessed. Additionally, molecular docking studies were conducted to elucidate the binding interactions of the synthesized derivatives within the cathepsin C active site. The results highlight promising structural features for the design of effective enzyme inhibitors and provide a foundation for further optimization of fluorovinylphosphonate-based dipeptides.
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