Issue 19, 2003
From the journal:

Chemical Communications

Rapid screening by MALDI-TOF mass spectrometry to probe binding specificity at enzyme active sites†

Michael E. Webb,a   Elaine Stephens,a   Alison G. Smithb  and  Chris Abell*a  

* Corresponding authors

a University Chemical Laboratory, University of Cambridge, Lensfield Road, Cambridge, UK
E-mail: ca26@cam.ac.uk
Tel: +44 1223 336405

b Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge, UK

Abstract

The binding affinity of aspartate decarboxylase has been probed using MALDI-TOF spectrometry; adducts formed covalently in the active site were detected by MALDI-TOF mass spectrometry after incubation of the enzyme with a range of potential ligands in the presence of NaCNBH3; this has highighted key structural features which will aid design of potential inhibitors.

Graphical abstract: Rapid screening by MALDI-TOF mass spectrometry to probe binding specificity at enzyme active sites

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Article information

DOI
https://doi.org/10.1039/B308182F
Article type
Communication
Submitted
16 Jul 2003
Accepted
18 Aug 2003
First published
01 Sep 2003

Chem. Commun., 2003, 2416-2417

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Rapid screening by MALDI-TOF mass spectrometry to probe binding specificity at enzyme active sites

M. E. Webb, E. Stephens, A. G. Smith and C. Abell, Chem. Commun., 2003, 2416 DOI: 10.1039/B308182F

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