Acyclic nucleoside bis-phosphonates as potent inhibitors of 6-oxopurine phosphoribosyltransferases

Špaček, Petr; Keough, D. T.; Vrbková, Silvie; Slavětínská, Lenka; Janeba, Zlatko; Naesens, L.; Edstein, M. D.; Chavchich, M.; Wang, T. H.; de Jersey, J.; Guddat, L. W.; Hocková, Dana

Number of the records: 1

Acyclic nucleoside bis-phosphonates as potent inhibitors of 6-oxopurine phosphoribosyltransferases

1.

SYSNO ASEP	0429113
Document Type	C - Proceedings Paper (int. conf.)
R&D Document Type	The record was not marked in the RIV
Title	Acyclic nucleoside bis-phosphonates as potent inhibitors of 6-oxopurine phosphoribosyltransferases
Author(s)	Špaček, Petr (UOCHB-X)_RID Keough, D. T. (AU) Vrbková, Silvie (UOCHB-X) Slavětínská, Lenka (UOCHB-X)_RID Janeba, Zlatko (UOCHB-X)_{RID, ORCID} Naesens, L. (BE) Edstein, M. D. (AU) Chavchich, M. (AU) Wang, T. H. (AU) de Jersey, J. (AU) Guddat, L. W. (AU) Hocková, Dana (UOCHB-X)_{RID, ORCID}
Number of authors	12
Source Title	Chemistry of Nucleic Acid Components. 16th Symposium. - Praha : Institute of Organic Chemistry and Biochemistry AS CR, v. v. i, 2014 / Hocek M. - ISBN 978-80-86241-50-0
Pages	s. 375-376
Number of pages	2 s.
Publication form	Print - P
Action	Symposium on Chemistry of Nucleic Acid Components /16./
Event date	08.06.2014-13.06.2014
VEvent location	Český Krumlov
Country	CZ - Czech Republic
Event type	EUR
Language	eng - English
Country	CZ - Czech Republic
Keywords	nucleotide analogues ; enzyme inhibitors ; Plasmodium
Subject RIV	CC - Organic Chemistry
R&D Projects	GAP207/11/0108 GA ČR - Czech Science Foundation (CSF)
Institutional support	UOCHB-X - RVO:61388963
Annotation	Hypoxanthine-guanin-(xanthine) phosphoribosyltransferase (HG(X)PRT) is critical for the survival of malarial parasites Plasmodium falciparum and Plasmodium vivax. These parasites rely on HG(X)PRT to make 6-oxopurine nucleoside monophosphates. Specific acyclic nucleoside phosphonates (ANPs) inhibit HG(X)PRT and thus have an anti-plasmodial activity. Crystal structures of human HGPRT in complex with several ANP-based inhibitors suggested that attachment of the second phosphonate group which could occupy the pyrophosphate binding site may lead to increased affinity of these compounds.
Workplace	Institute of Organic Chemistry and Biochemistry
Contact	asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418
Year of Publishing	2015

Number of the records: 1