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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Chemical Communications

Issue 92, 2012

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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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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

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

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

DOI: 10.1039/C2CC36044F
Received 20 Aug 2012, Accepted 14 Sep 2012
First published online 18 Sep 2012

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

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