Nuclear magnetic resonance studies on wheat germ agglutinin-monomeric amino sugar interactions

TY - JOUR

T1 - Nuclear magnetic resonance studies on wheat germ agglutinin-monomeric amino sugar interactions

AU - Jordan, Frank

AU - Bahr, Hanae

AU - Patrick, John

AU - Woo, Peter W.K.

N1 - Funding Information: Frank Jordan thanks the Rutgers University Council and Biomedical Research Support for Financial Assistance as well as Dr. William Redwood for acquainting him with the importance of WGA.

PY - 1981/3

Y1 - 1981/3

N2 - The interaction of several N-acetyl-d-glucosamine analogs and of sialyl lactose with the lectin wheat germ agglutinin was studied by nuclear magnetic resonance. N-2H3-acetyl-d-gluocosamine was synthesized and found to displace the N-acetyl methyl signal toward its free chemical shift in N-acetylglucosamine and N-acetylneuraminic acid demonstrating common binding sites for the latter two compounds. The N-acetyl methyl signal of the α-methylglucoside of N-acetylglucosamine could be titrated but a 3-deoxy analog could not, the latter exhibiting very weak binding and demonstrating the importance of the 3-OH group in the binding process. Sialyl lactose (an N-acetylneuraminic acid analog) was rather tightly bound to the lectin. N-F3-acetyl-d-glucosamine was synthesized and its binding to the lectin was studied at pH 4, 4.5, 5.1 by 19F NMR. The two anomers were found to bind with nearly equal Kd′s but exhibited a pH and anomer dependent Δ (total bound chemical shift). The -CF3 analog was found to bind considerably stronger to the lectin than the -CH3 compound. The clear resolution of the α and β anomers of this molecule make it a very useful probe of the lectin binding site.

AB - The interaction of several N-acetyl-d-glucosamine analogs and of sialyl lactose with the lectin wheat germ agglutinin was studied by nuclear magnetic resonance. N-2H3-acetyl-d-gluocosamine was synthesized and found to displace the N-acetyl methyl signal toward its free chemical shift in N-acetylglucosamine and N-acetylneuraminic acid demonstrating common binding sites for the latter two compounds. The N-acetyl methyl signal of the α-methylglucoside of N-acetylglucosamine could be titrated but a 3-deoxy analog could not, the latter exhibiting very weak binding and demonstrating the importance of the 3-OH group in the binding process. Sialyl lactose (an N-acetylneuraminic acid analog) was rather tightly bound to the lectin. N-F3-acetyl-d-glucosamine was synthesized and its binding to the lectin was studied at pH 4, 4.5, 5.1 by 19F NMR. The two anomers were found to bind with nearly equal Kd′s but exhibited a pH and anomer dependent Δ (total bound chemical shift). The -CF3 analog was found to bind considerably stronger to the lectin than the -CH3 compound. The clear resolution of the α and β anomers of this molecule make it a very useful probe of the lectin binding site.

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U2 - https://doi.org/10.1016/0003-9861(81)90011-4

DO - https://doi.org/10.1016/0003-9861(81)90011-4

M3 - Article

C2 - 6894523

VL - 207

SP - 81

EP - 86

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -