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The interaction of N-trifluoroacetylgalactosamine and its derivatives with winged bean (Psophocarpus tetragonolobus) basic agglutinin reveals differential mechanism of their recognition: a fluorine-19 nuclear magnetic resonance study

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Abstract

Here, we show the binding results of a leguminosae lectin, winged bean basic agglutinin (WBA I) to N-trifluoroacetylgalactosamine (NTFAGalN), methyl-α-N-trifluoroacetylgalactosamine (MeαNTFAGalN) and methyl-β-tifluoroacetylgalactosamine (MeβNTFAGalN) using 19 F NMR spectroscopy. No chemical shift difference between the free and bound states for NTFAGalN and MeβNTFAGalN, and 0.01-ppm chemical shift change for MeαNTFAGalN, demonstrate that the MeαNTFAGalN has a sufficiently long residence time on the protein binding site as compared to MeβNTFAGalN and the free anomers of NTFAGalN. The sugar anomers were found in slow exchange with the binding site of agglutinin. Consequently, we obtained their binding parameters to the protein using line shape analyses. Aforementioned analyses of the activation parameters for the interactions of these saccharides indicate that the binding of α and β anomers of NTFAGalN and MeαNTFAGalN is controlled enthalpically, while that of MeβNTFAGalN is controlled entropically. This asserts the sterically constrained nature of the interaction of the MeβNTFAGalN with WBA I. These studies thus highlight a significant role of the conformation of the monosaccharide ligands for their recognition by WBA I.

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Abbreviations

NMR:

Nuclear Magnetic Resonance

WBA I:

Winged bean basic agglutinin

NTFAGalN:

N-trifluoroactylgalactosamine

MeαNTFAGalN:

Methyl-α-N-trifluoroacetylgalactosamine

MeβNTFAGalN:

Methyl-β-tifluoroacetylgalactosamine

PNA:

Peanut agglutinin

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Acknowledgments

This work is supported by the Department of Science and Technology and Council of Scientific and Industrial Research (CSIR), Government of India to AS. AS is Bhatnagar Fellow of CSIR. SK is a Research Associate of CSIR and Amrita Singh is a SRF of University Grants Commission (UGC). We thank the Sophisticated Instruments Facility at Indian Institute of Science, Bangalore, for the use of Bruker WH – 400 MHz NMR spectrometer.

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  1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012, India

    Samiksha Katiyar, Amrita Singh & Avadhesha Surolia

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  1. Samiksha Katiyar
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  2. Amrita Singh
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Correspondence to Avadhesha Surolia.

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Katiyar, S., Singh, A. & Surolia, A. The interaction of N-trifluoroacetylgalactosamine and its derivatives with winged bean (Psophocarpus tetragonolobus) basic agglutinin reveals differential mechanism of their recognition: a fluorine-19 nuclear magnetic resonance study. Glycoconj J 31, 537–543 (2014). https://doi.org/10.1007/s10719-014-9545-7

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