Biotin-c10-AppCH(2)ppA is an effective new chemical proteomics probe for diadenosine polyphosphate binding proteins

M. Ameruddin Azhar, Michael Wright, Ahmed Kamal, Judith Nagy, Andrew D. Miller*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

Here we report on the synthesis of a synthetic, stable biotin-c10-AppCH(2)ppA conjugate involving an unusual Cannizzaro reaction step. This conjugate is used to bind prospective AP(4)A binding proteins from Escherichia coil 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 AP(4)A-binding proteins. Therefore these hits represent a sound basis on which to construct new hypotheses concerning the cellular importance of AP(4)A to bacterial cells and the potential biological significance of AP(4)A-protein binding interactions.

Original languageEnglish
Pages (from-to)2928-2933
Number of pages6
JournalBIOORGANIC AND MEDICINAL CHEMISTRY LETTERS
Volume24
Issue number13
DOIs
Publication statusPublished - 1 Jul 2014

Keywords

  • Chemical proteomics
  • Dinucleoside polyphosphates
  • Diadenosine tetraphosphate analogues
  • AP(4)A binding proteins
  • Estherichia coli
  • ESCHERICHIA-COLI
  • TRANSCRIPTIONAL REGULATOR
  • SUBSTRATE-SPECIFICITY
  • MASS-SPECTROMETRY
  • CRYSTAL-STRUCTURE
  • MALTOSE REGULON
  • EXPRESSION
  • IDENTIFICATION
  • OXIDOREDUCTASE
  • BIOSYNTHESIS

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