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Water envelope has a critical impact on the design of protein-protein interaction inhibitors.
Chem. Commun. 56, 4360-4363 (2020)
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Research data
DOI
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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Times Cited
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5.996
1.144
3
4
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Binding-affinity; Molecules; Thermodynamics; Solvent; Surface; Energy
Language
english
Publication Year
2020
HGF-reported in Year
2020
ISSN (print) / ISBN
0009-241X
e-ISSN
1364-548X
Journal
Chemical Communications
Quellenangaben
Volume: 56,
Issue: 31,
Pages: 4360-4363
Publisher
Royal Society of Chemistry (RSC)
Publishing Place
Thomas Graham House, Science Park, Milton Rd, Cambridge Cb4 0wf, Cambs, England
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Enabling and Novel Technologies
PSP Element(s)
G-503000-001
WOS ID
WOS:000528059600021
Scopus ID
85083561793
Erfassungsdatum
2020-05-08