Electrostatic similarities between protein and small molecule ligands facilitate the design of protein-protein interaction inhibitors.

One of the underlying principles in drug discovery is that a biologically active compound is complimentary in shape and molecular recognition features to its receptor. This principle infers that molecules binding to the same receptor may share some common features. Here, we have investigated whether...

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Autores principales:	Arnout Voet, Francois Berenger, Kam Y J Zhang
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ec45505f8aa64ca6afd98e438ef509d8
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spelling	oai:doaj.org-article:ec45505f8aa64ca6afd98e438ef509d82021-11-18T08:51:40ZElectrostatic similarities between protein and small molecule ligands facilitate the design of protein-protein interaction inhibitors.1932-620310.1371/journal.pone.0075762https://doaj.org/article/ec45505f8aa64ca6afd98e438ef509d82013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24130741/?tool=EBIhttps://doaj.org/toc/1932-6203One of the underlying principles in drug discovery is that a biologically active compound is complimentary in shape and molecular recognition features to its receptor. This principle infers that molecules binding to the same receptor may share some common features. Here, we have investigated whether the electrostatic similarity can be used for the discovery of small molecule protein-protein interaction inhibitors (SMPPIIs). We have developed a method that can be used to evaluate the similarity of electrostatic potentials between small molecules and known protein ligands. This method was implemented in a software called EleKit. Analyses of all available (at the time of research) SMPPII structures indicate that SMPPIIs bear some similarities of electrostatic potential with the ligand proteins of the same receptor. This is especially true for the more polar SMPPIIs. Retrospective analysis of several successful SMPPIIs has shown the applicability of EleKit in the design of new SMPPIIs.Arnout VoetFrancois BerengerKam Y J ZhangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 10, p e75762 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Arnout Voet Francois Berenger Kam Y J Zhang Electrostatic similarities between protein and small molecule ligands facilitate the design of protein-protein interaction inhibitors.
description	One of the underlying principles in drug discovery is that a biologically active compound is complimentary in shape and molecular recognition features to its receptor. This principle infers that molecules binding to the same receptor may share some common features. Here, we have investigated whether the electrostatic similarity can be used for the discovery of small molecule protein-protein interaction inhibitors (SMPPIIs). We have developed a method that can be used to evaluate the similarity of electrostatic potentials between small molecules and known protein ligands. This method was implemented in a software called EleKit. Analyses of all available (at the time of research) SMPPII structures indicate that SMPPIIs bear some similarities of electrostatic potential with the ligand proteins of the same receptor. This is especially true for the more polar SMPPIIs. Retrospective analysis of several successful SMPPIIs has shown the applicability of EleKit in the design of new SMPPIIs.
format	article
author	Arnout Voet Francois Berenger Kam Y J Zhang
author_facet	Arnout Voet Francois Berenger Kam Y J Zhang
author_sort	Arnout Voet
title	Electrostatic similarities between protein and small molecule ligands facilitate the design of protein-protein interaction inhibitors.
title_short	Electrostatic similarities between protein and small molecule ligands facilitate the design of protein-protein interaction inhibitors.
title_full	Electrostatic similarities between protein and small molecule ligands facilitate the design of protein-protein interaction inhibitors.
title_fullStr	Electrostatic similarities between protein and small molecule ligands facilitate the design of protein-protein interaction inhibitors.
title_full_unstemmed	Electrostatic similarities between protein and small molecule ligands facilitate the design of protein-protein interaction inhibitors.
title_sort	electrostatic similarities between protein and small molecule ligands facilitate the design of protein-protein interaction inhibitors.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/ec45505f8aa64ca6afd98e438ef509d8
work_keys_str_mv	AT arnoutvoet electrostaticsimilaritiesbetweenproteinandsmallmoleculeligandsfacilitatethedesignofproteinproteininteractioninhibitors AT francoisberenger electrostaticsimilaritiesbetweenproteinandsmallmoleculeligandsfacilitatethedesignofproteinproteininteractioninhibitors AT kamyjzhang electrostaticsimilaritiesbetweenproteinandsmallmoleculeligandsfacilitatethedesignofproteinproteininteractioninhibitors
_version_	1718421236549156864

Electrostatic similarities between protein and small molecule ligands facilitate the design of protein-protein interaction inhibitors.

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