Reaching for high-hanging fruit in drug discovery at protein–protein interfaces

James A. Wells and Christopher L. McClendon
Additional contact information
James A. Wells: University of California at San Francisco
Christopher L. McClendon: Graduate Group in Biophysics, University of California at San Francisco

Nature, 2007, vol. 450, issue 7172, 1001-1009

Abstract: Abstract Targeting the interfaces between proteins has huge therapeutic potential, but discovering small-molecule drugs that disrupt protein–protein interactions is an enormous challenge. Several recent success stories, however, indicate that protein–protein interfaces might be more tractable than has been thought. These studies discovered small molecules that bind with drug-like potencies to 'hotspots' on the contact surfaces involved in protein–protein interactions. Remarkably, these small molecules bind deeper within the contact surface of the target protein, and bind with much higher efficiencies, than do the contact atoms of the natural protein partner. Some of these small molecules are now making their way through clinical trials, so this high-hanging fruit might not be far out of reach.

Date: 2007
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/nature06526 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:450:y:2007:i:7172:d:10.1038_nature06526

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature06526

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().