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

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• 作者：M. Ameruddin Azhar^a ; ^b ; Michael Wright^a ; ^c ; Ahmed Kamal^b ; Judith Nagy^d ; Andrew D. Miller^a ; ^c ; ^{a.miller07@btinternet.com" class="auth_mail} ; ^{andrew.miller@globalacorn.com" class="auth_mail}
• 关键词：Chemical proteomics ; Dinucleoside polyphosphates ; Diadenosine tetraphosphate analogues ; Ap4A binding proteins ; Escherichia coli
• 刊名：Bioorganic and Medicinal Chemistry Letters
• 出版年：1 July 2014
• 年：2014
• 卷：24
• 期：13
• 页码：2928-2933
• 全文大小：691 K

文摘

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.