First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP5 kinase

Andrew M. Riley; Huanchen Wang; Jeremy D. Weaver; Stephen B. Shears; Barry V. L. Potter

doi:10.1039/C2CC36044F

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First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP₅ kinase†

Andrew M. Riley,^a Huanchen Wang,^b Jeremy D. Weaver,^b Stephen B. Shears^b and Barry V. L. Potter*^a

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* Corresponding authors

^a Wolfson Laboratory of Medicinal Chemistry, Department of Pharmacy and Pharmacology, University of Bath, UK
E-mail: b.v.l.potter@bath.ac.uk
Fax: +44 (0)1225 386114
Tel: +44 (0)1225 386639

^b Inositol Signaling Group, Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina, USA

Abstract

We synthesised analogues of diphosphoinositol polyphosphates (PP-InsPs) in which the diphosphate is replaced by an α-phosphonoacetic acid (PA) ester. Structural analysis revealed that 5-PA-InsP₅ mimics 5-PP-InsP₅ binding to the kinase domain of PPIP5K2; both molecules were phosphorylated by the enzyme. PA-InsPs are promising candidates for further studies into the biology of PP-InsPs.

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Article information

DOI: https://doi.org/10.1039/C2CC36044F
Article type: Communication
Submitted: 20 Aug 2012
Accepted: 14 Sep 2012
First published: 18 Sep 2012
This article is Open Access

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Chem. Commun., 2012,48, 11292-11294

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First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP₅ kinase

A. M. Riley, H. Wang, J. D. Weaver, S. B. Shears and B. V. L. Potter, Chem. Commun., 2012, 48, 11292 DOI: 10.1039/C2CC36044F

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