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Default 1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a suga

1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.

Related Articles 1H NMR study of the interaction of N,N',N"-triacetyl chitotriose with Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.

FEBS Lett. 1995 Aug 21;370(3):245-9

Authors: Verheyden P, Pletinckx J, Maes D, Pepermans HA, Wyns L, Willem R, Martins JC

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.

PMID: 7656986 [PubMed - indexed for MEDLINE]



Source: PubMed
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