Document Detail


Arylaminoethyl amides as noncovalent inhibitors of cathepsin S. Part 2: Optimization of P1 and N-aryl.
MedLine Citation:
PMID:  16412634     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A systematic study of anilines led to the discovery of a metabolically robust fluoroindoline replacement for the alkoxy aniline toxicophore in 1. Investigations of the P1 pocket resulted in the discovery of a wide tolerance of functionality leading to the discovery of 11 as a potent and selective inhibitor of cathepsin S.
Authors:
Phillip B Alper; Hong Liu; Arnab K Chatterjee; KhanhLinh T Nguyen; David C Tully; Christine Tumanut; Jun Li; Jennifer L Harris; Tove Tuntland; Jonathan Chang; Perry Gordon; Thomas Hollenbeck; Donald S Karanewsky
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Publication Detail:
Type:  Journal Article     Date:  2006-01-18
Journal Detail:
Title:  Bioorganic & medicinal chemistry letters     Volume:  16     ISSN:  0960-894X     ISO Abbreviation:  Bioorg. Med. Chem. Lett.     Publication Date:  2006 Mar 
Date Detail:
Created Date:  2006-02-07     Completed Date:  2006-04-17     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9107377     Medline TA:  Bioorg Med Chem Lett     Country:  England    
Other Details:
Languages:  eng     Pagination:  1486-90     Citation Subset:  IM    
Affiliation:
Genomics Institute of the Novartis Research Foundation, 10675 John J. Hopkins Dr., San Diego, CA 92121, USA. palper@gnf.org
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MeSH Terms
Descriptor/Qualifier:
Amides / chemical synthesis,  chemistry,  pharmacology*
Amination
Benzene Derivatives / chemical synthesis,  chemistry,  pharmacology
Binding Sites
Cathepsin K
Cathepsin L
Cathepsins / antagonists & inhibitors*,  chemistry,  metabolism
Cysteine Endopeptidases / chemistry,  metabolism
Cysteine Proteinase Inhibitors / chemical synthesis,  chemistry,  pharmacology*
Drug Design*
Ethanol / chemistry
Inhibitory Concentration 50
Models, Molecular
Molecular Structure
Structure-Activity Relationship
Chemical
Reg. No./Substance:
0/Amides; 0/Benzene Derivatives; 0/Cysteine Proteinase Inhibitors; 64-17-5/Ethanol; EC 3.4.-/Cathepsins; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.15/Cathepsin L; EC 3.4.22.27/cathepsin S; EC 3.4.22.38/Cathepsin K

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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