Inhibitors of HIV-1 Protease by Using In Situ Click Chemistry

Twice poor equals potent: HIV‐1 Protease assembles its own potent inhibitor through formation of the triazole linkage from azide‐ and alkyne‐containing fragments that are themselves poor binders.

Saved in:
Bibliographic Details
Published inAngewandte Chemie International Edition Vol. 45; no. 9; pp. 1435 - 1439
Main Authors Whiting, Matthew, Muldoon, John, Lin, Ying-Chuan, Silverman, Steven M., Lindstrom, William, Olson, Arthur J., Kolb, Hartmuth C., Finn, M. G., Sharpless, K. Barry, Elder, John H., Fokin, Valery V.
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 20.02.2006
WILEY‐VCH Verlag
Subjects
Chromatography, High Pressure Liquid - methods
click chemistry
Combinatorial Chemistry Techniques
drug design
HIV Protease Inhibitors - chemical synthesis
HIV Protease Inhibitors - chemistry
HIV-1 protease
inhibitors
Mass Spectrometry - methods
Molecular Conformation
Sensitivity and Specificity
Stereoisomerism
Time Factors
triazoles
Online AccessGet full text

Cover

More Information
Summary:Twice poor equals potent: HIV‐1 Protease assembles its own potent inhibitor through formation of the triazole linkage from azide‐ and alkyne‐containing fragments that are themselves poor binders.
Bibliography:istex:D1BF4A04A712CD1CB7C2320B5EBD111288776E57
We thank the National Institute of General Medical Sciences, the National Institutes of Health (GM048870), the Skaggs Institute for Chemical Biology, and the W. M. Keck Foundation (K.B.S.) for financial support.
ArticleID:ANIE200502161
ark:/67375/WNG-7626QCKG-D
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200502161