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Biotin-c10-AppCH2ppA is an effective new chemical proteomics probe for diadenosine polyphosphate binding proteins.

Authors :
Azhar, M. Ameruddin
Wright, Michael
Kamal, Ahmed
Nagy, Judith
Miller, Andrew D.
Source :
Bioorganic & Medicinal Chemistry Letters. Jul2014, Vol. 24 Issue 13, p2928-2933. 6p.
Publication Year :
2014

Abstract

Abstract: Here we report on the synthesis of a synthetic, stable biotin-c10-AppCH2ppA conjugate involving an unusual Cannizzaro reaction step. This conjugate is used to bind prospective Ap4A binding proteins from Escherichia coli bacterial cell lyzates. Following binding, identities of these proteins are then determined smoothly by a process of magnetic bio-panning and electrospray mass spectrometry. Protein hits appear to be a definitive set of stress protein related targets. While this hit list may not be exclusive, and may vary with the nature of sampling conditions and organism status, nevertheless hits do appear to correspond with bona fide Ap4A-binding proteins. Therefore these hits represent a sound basis on which to construct new hypotheses concerning the cellular importance of Ap4A to bacterial cells and the potential biological significance of Ap4A-protein binding interactions. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
0960894X
Volume :
24
Issue :
13
Database :
Academic Search Index
Journal :
Bioorganic & Medicinal Chemistry Letters
Publication Type :
Academic Journal
Accession number :
96232050
Full Text :
https://doi.org/10.1016/j.bmcl.2014.04.076