Design of potent inhibitors of human beta-secretase. Part 2

Autor:	Donna J. Paddock, Alfredo G. Tomasselli, John N. Freskos, Heintz Robert M, Brown David L, Thomas L. Emmons, Joseph B. Moon, Timothy E. Benson, Yvette M. Fobian, John M. Molyneaux, Alice Laborde, Greg Winterrowd, D. Bryan Prince, Brent V. Mischke, Joseph J. McDonald, Michael J. Bienkowski, Patrick B. Mullins
Rok vydání:	2006
Předmět:	Cellular activity Stereochemistry Clinical Biochemistry Pharmaceutical Science Biochemistry Structure-Activity Relationship Protein structure Alzheimer Disease Drug Discovery Hydrolase Side chain Structure–activity relationship Humans Protease Inhibitors Beta (finance) Molecular Biology Cells Cultured Sulfonamides biology Molecular Structure Chemistry Organic Chemistry Combinatorial chemistry Drug Design biology.protein β secretase Molecular Medicine Carbamates Amyloid Precursor Protein Secretases Amyloid precursor protein secretase
Zdroj:	Bioorganicmedicinal chemistry letters. 17(1)
ISSN:	0960-894X
Popis:	We describe an optimized series of acyclic hydroxyethylamine transition state isosteres of beta-secretase that incorporates a variety of P(2) side chains that yield potent inhibitors with excellent cellular activity. A 2.2A crystal structure of compound 13 is shown.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1541d1cca9874f925ad126ae4a925af1 https://pubmed.ncbi.nlm.nih.gov/17049233 Zobrazit plný text záznamu Full Text from ScienceDirect