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1 H NMR study of the interaction of N , N ′, N ″‐triacetyl chitotriose with Ac‐AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus
Author(s) -
Verheyden Patricia,
Pletinckx Jurgen,
Maes Dominique,
Pepermans Henri A.M.,
Wyns Lode,
Willem Rudolph,
Martins JoséC.
Publication year - 1995
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 - 10.1016/0014-5793(95)00835-w
Subject(s) - chemistry , nuclear magnetic resonance spectroscopy , stereochemistry
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 1 H 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 K a . The most pronounced shifts occur mainly in the C‐terminal half of the sequence. They involve the aromatic residues Phe 18 , Tyr 20 and Tyr 27 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.