A FTIR spectroscopy evidence of the interactions between wheat germ agglutinin and N-acetylglucosamine residues.
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 alpha-helices and beta-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 alpha-helices and a concomitant appearance of beta-sheets, inducing more or less peptidic N-H deuteration.
Bonnin
S
S
Laboratoire de Physico-chimie biologique, CNRS UPRESA 5013, Université Claude Bernard, Lyon I, Villeurbanne, France.
Besson
F
F
Gelhausen
M
M
Chierici
S
S
Roux
B
B
D000117:Acetylglucosamine / Q000737:chemistry / Q000378:metabolism*; D006017:Glycolipids / Q000737:chemistry / Q000378:metabolism; D008081:Liposomes / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D017550:Spectroscopy, Fourier Transform Infrared; D014909:Wheat Germ Agglutinins / Q000737:chemistry* / Q000378:metabolism*
D006017:Glycolipids; D008081:Liposomes; D014909:Wheat Germ Agglutinins; D000117:Acetylglucosamine