Effect of substituents on the thermodynamics of D-galactopyranoside binding to winged bean (Psophocarpus tetragonolobus) basic lectin

Swaminathan, CP and Gupta, D and Sharma, V and Surolia, Avadhesa (1997) Effect of substituents on the thermodynamics of D-galactopyranoside binding to winged bean (Psophocarpus tetragonolobus) basic lectin. In: Biochemistry, 36 (43). pp. 13428-13434.

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Abstract

Isothermal titration calorimetric measurements of the binding of deoxy, fluorodeoxy, and methoxy derivatives of D-galactopyranoside (alpha-D-Gal) to the basic lectin from winged bean Psophocarpus tetragonolobus, WBA I, have been carried out. Each of the ligands binding to WBA I displayed the same stoichiometry of one per subunit (29 kDa) of WBA I. The binding enthalpies for various derivatives are essentially independent of temperature and show complementary changes with respect to binding entropies. Replacement of the hydroxyl group by fluorine or hydrogen on C3 and C4 of the galactopyranoside eliminates binding to the lectin, consistent with C3-OH and C4-OH acting as hydrogen bond donors. The affinity for C2 derivatives of galactose decreases in the order GalNAc > 2MeOGal > 2FGal congruent to Gal > 2HGal, which suggests that both polar and nonpolar residues surround the C2 locus of galactose, consistent with the observed high affinity of WBA I toward GalNAc where the acetamido group at C2 position is probably stabilized by both nonpolar interactions with the methyl group and polar interactions with the carbonyl group. The binding of C6 derivatives follows the order Gal > 6FGal > D-Fuc much greater than 6MeOGal congruent to L-Ara, indicating the presence of favourable polar interactions with a hydrogen bond donor in the vicinity. On the basis of these results the hydrogen bond donor-acceptor relationship of the complexation of methyl-alpha-D-galactopyranoside with the primary combining site of WBA I is proposed.

Item Type:	Journal Article
Publication:	Biochemistry
Publisher:	American Chemical Society
Additional Information:	Copyright of this article belongs to American Chemical Society.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	02 Jun 2009 10:12
Last Modified:	19 Sep 2010 05:25
URI:	http://eprints.iisc.ac.in/id/eprint/18903

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