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Ratkova, E.L. ; Dawidowski, M. ; Napolitano, V.* ; Dubin, G.* ; Fino, R. ; Ostertag, M.S. ; Sattler, M. ; Popowicz, G.M. ; Tetko, I.V.

Water envelope has a critical impact on the design of protein-protein interaction inhibitors.

Chem. Commun. 56, 4360-4363 (2020)
Postprint DOI
Open Access Green
We show that a water envelope network plays a critical role in protein-protein interactions (PPI). The potency of a PPI inhibitor is modulated by orders of magnitude on manipulation of the solvent envelope alone. The structure-activity relationship of PEX14 inhibitors was analyzed as an example using in silico and X-ray data.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Binding-affinity; Molecules; Thermodynamics; Solvent; Surface; Energy
ISSN (print) / ISBN 0009-241X
e-ISSN 1364-548X
Journal Chemical Communications
Quellenangaben Volume: 56, Issue: 31, Pages: 4360-4363 Article Number: , Supplement: ,
Publisher Royal Society of Chemistry (RSC)
Publishing Place Thomas Graham House, Science Park, Milton Rd, Cambridge Cb4 0wf, Cambs, England
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)