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A FTIR spectroscopy evidence of the interactions between wheat germ agglutinin and N ‐acetylglucosamine residues
Author(s) -
Bonnin Stéphanie,
Besson Françoise,
Gelhausen Micaèle,
Chierici Sabine,
Roux Bernard
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00981-3
Subject(s) - wheat germ agglutinin , fourier transform infrared spectroscopy , chemistry , spectroscopy , infrared spectroscopy , stereochemistry , carbohydrate conformation , nuclear magnetic resonance spectroscopy , crystallography , biochemistry , lectin , organic chemistry , physics , quantum mechanics
Wheat germ agglutinin (WGA), a lectin binding a N ‐acetyl‐ D ‐neuraminic acid (NeuNAc) and/or N ‐acetyl‐ D ‐glucosamine (GlcNAc) group, was studied by Fourier transform infrared (FTIR) spectroscopy. Deconvolution of the FTIR spectrum of WGA alone indicated the presence of few α‐helices and β‐sheets, in contrast to many other lectins. These results agree with previous WGA crystal data. The WGA conformational changes, induced by GlcNAc‐bearing liposomes or GlcNAc oligomers, were studied by infrared differential spectroscopy. The GlcNAc binding to WGA resulted in a decrease of turns and α‐helices and a concomitant appearance of β‐sheets, inducing more or less peptidic N‐H deuteration.