A number of potential matrix candidates were investigated with regard to the importance of the pH in the matrixassisted laser desorption/ionization mass spectrometry (MALDI/MS) analysis of non-covalently bound protein complexes. The matrices examined were 2,5-dihydroxybenzoic acid (DHB), 4-hydroxy-a
Study of peptide–sugar non-covalent complexes by infrared atmospheric pressure matrix-assisted laser desorption/ionization
✍ Scribed by Christopher E. Von Seggern; Robert J. Cotter
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 262 KB
- Volume
- 39
- Category
- Article
- ISSN
- 1076-5174
- DOI
- 10.1002/jms.644
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✦ Synopsis
Abstract
Infrared atmospheric pressure matrix‐assisted laser desorption/ionization quadrupole ion trap mass spectrometry was applied to the study of siglec binding to oligosaccharide ligands. Peptides were designed to mimic the binding sites of three members of the siglec family: sialoadhesin, MAG and CD22. These peptides were tested for their ability to complex with their carbohydrate ligands 3^′^‐sialyllactose (3^′^SL) and 6^′^‐sialyllactose (6^′^SL). All peptides demonstrated the ability to bind to the carbohydrates, with the peptide representing sialoadhesin maintaining its binding specificity for 3^′^SL in preference to 6^′^SL. This technique can be used to study other protein–sugar interactions and can be expanded to create high‐throughput screening techniques. Copyright © 2004 John Wiley & Sons, Ltd.
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