A FTIR spectroscopy evidence of the interactions between wheat germ agglutinin and N‐acetylglucosamine residues

FEBS Letters

Gelhausen, Micaèle²  Chierici, Sabine¹  Besson, Françoise²  Roux, Bernard²  Bonnin, Stéphanie² 

[1] Laboratoire de Chimie organique 2, CNRS UMR 5622, Université Claude Bernard, Villeurbanne, France;Laboratoire de Physico-chimie biologique, CNRS UPRESA 5013, Université Claude Bernard, Lyon I, Bat. 303, 43 Boulevard du 11 Novembre 1918, 69622 Villeurbanne Cedex, France

关键词: Fourier transform infrared spectroscopy;    Hydrogen bond;    Lectin interaction;    N-acetyl-D-glucosamine;    Neoglycolipid;    DMPC;    dimyristoylphosphatidylcholine;    2H2O buffer;    10 mM Tris-HCl buffer in 2H2O pH 7.5;    FTIR;    Fourier transform infrared;    GlcNAc;    N-acetyl-D-glucosamine;    NeuNAc;    N-acetyl-D-neuraminic acid;    NG;    neoglycolipid;    WGA;    wheat germ agglutinin;   

DOI  :  10.1016/S0014-5793(99)00981-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown