H NMR study of the interaction of N,N′,N″-triacetyl chitotriose with Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus |
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Authors: | Patricia Verheyden Jurgen Pletinckx Dominique Maes Henri A M Pepermans Lode Wyns Rudolph Willem JosC Martins |
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Institution: | Patricia Verheyden, Jurgen Pletinckx, Dominique Maes, Henri A. M. Pepermans, Lode Wyns, Rudolph Willem,JoséC. Martins |
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Abstract: | The interaction between Ac-AMP2, a lectin-like small protein with antimicrobial and antifungal activity isolated from Amaranthus caudatus, and N,N′,N″-triacetyl chitotriose was studied using 1H NMR spectroscopy. Changes in chemical shift and line width upon increasing concentration of N,N′,N″-triacetyl chitotriose to Ac-AMP2 solutions at pH 6.9 and 2.4 were used to determine the interaction site and the association constant Ka. The most pronounced shifts occur mainly in the C-terminal half of the sequence. They involve the aromatic residues Phe18, Tyr20 and Tyr27 together with their surrounding residues, as well as the N-terminal Val-Gly-Glu segment. Several NOEs between Ac-AMP2 and the N,N′,N″-triacetyl chitotriose resonances are reported. |
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Keywords: | Ac-AMP2 N N′ N″-triacetyl chitotriose Protein-carbohydrate interaction 1H NMR Lectin |
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