التفاصيل البيبلوغرافية
العنوان:
Azepanone-based inhibitors of human cathepsin S: optimization of selectivity via the P2 substituent
المؤلفون:
Jeffrey K. Kerns , Widdowson Katherine L , Patricia L. Podolin , Paul M. Keller , Benoit Riflade , Neysa Nevins , Attiq Rahman , Dennis S. Yamashita , Qi Jin , Bondinell William E , Thaddeus A. Tomaszek , Xiaoyang Dong , Laura Mitchell , Hong Nie , Donald C. Carpenter
المصدر:
Bioorganicmedicinal chemistry letters . 21(15)
سنة النشر:
2011
مصطلحات موضوعية:
Niacinamide , Stereochemistry , Cathepsin L , Clinical Biochemistry , Cathepsin K , Substituent , Pharmaceutical Science , Biochemistry , chemistry.chemical_compound , Structure-Activity Relationship , Cathepsin O , Drug Discovery , Structure–activity relationship , Humans , Computer Simulation , Protease Inhibitors , Molecular Biology , Cathepsin S , Alanine , Binding Sites , Nicotinamide , biology , Chemistry , Organic Chemistry , Stereoisomerism , Azepines , Cathepsins , biology.protein , Molecular Medicine , Selectivity
الوصف:
A series of azepanone inhibitors of cathepsin S is described. Selectivity over both cathepsin K and cathepsin L was achieved by varying the P2 substituent. Ultimately, a balanced potency and selectivity profile was achieved in compound 39 possessing a 1-methylcyclohexyl alanine at P2 and nicotinamide as the P' substituent. The cellular potency of selected analogs is also described.
تدمد:
1464-3405
URL الوصول:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::847de7f88d648a695505d7aa3da93e11 https://pubmed.ncbi.nlm.nih.gov/21733692
حقوق:
CLOSED
رقم الأكسشن:
edsair.doi.dedup.....847de7f88d648a695505d7aa3da93e11
قاعدة البيانات:
OpenAIRE
