1H NMR study of the interaction of N,N′,N″‐triacetyl chitotriose with Ac‐AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus

Autor: Verheyden, Patricia, Pletinckx, Jurgen, Maes, Dominique, Pepermans, Henri A.M., Wyns, Lode, Willem, Rudolph, Martins, JoséC.
Zdroj: FEBS Letters; August 1995, Vol. 370 Issue: 3 p245-249, 5p
Abstrakt: 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 chitotrioseto 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, Tyr20and Tyr27together 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.
Databáze: Supplemental Index