选择性
二肽基肽酶
立体化学
化学
内酰胺
酶
组合化学
催化作用
生物化学
作者
Luís A. R. Carvalho,B. Ross,Lorenz Fehr,Oguz Bolgi,Svenja Wöhrle,Kenneth M. Lum,David Podlesainski,Andreia C. Vieira,R. Kiefersauer,Rita Félix,Tiago Rodrigues,Susana D. Lucas,Olaf Groß,Ruth Geiss‐Friedlander,Benjamin F. Cravatt,Robert Huber,Markus Kaiser,Rui Moreira
标识
DOI:10.1002/anie.202213804
摘要
A lone 4-oxo-β-lactam molecule moves towards the catalytic site of an illuminated dipeptidyl peptidase 8 (DPP8) in a vast universe of chemical space. Achieving DPP8/9 selectivity has remained a challenge in chemical biology. The 4-oxo-β-lactams, identified by a chemoproteomics platform as DPP8/9 inhibitors may hold the key to the highly sought DPP8/9 selectivity via an unprecedented DPP8-specific mechanism, as demonstrated through X-ray diffraction by Markus Kaiser, Rui Moreira et al. in their Research Article (DOI: 10.1002/anie.202210498).
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