Synthesis of beta-arabinofuranoside glycolipids, studies of their binding to surfactant protein-A and effect on sliding motilities of M. smegmatis

Naresh, Kottari and Avaji, Prakash Gouda and Maiti, Krishnagopal and Bharati, Binod Kumar and Syal, Kirtimaan and Chatterji, Dipankar and Jayaraman, Narayanaswamy (2012) Synthesis of beta-arabinofuranoside glycolipids, studies of their binding to surfactant protein-A and effect on sliding motilities of M. smegmatis. In: Glycoconjugate Journal, 29 (2-3). pp. 107-118.

PDF Synthesis.pdf - Published Version Restricted to Registered users only Download (573kB) | Request a copy

Abstract

Surfactant protein A (SP-A), which is a lung innate immune system component, is known to bind glycolipids present at the cell surface of a mycobacterial pathogen. Lipoarabinomannan (LAM), a component of mycobacterial thick, waxy cell wall, is one of the glycolipid ligands for SP-A. In order to assess binding of synthetic glycolipids with SP-A and the glycosidic linkage preferences for the interaction, beta-arabinofuranoside trisaccharide glycolipids constituted with beta-(1 -> 2), beta-(1 -> 3) and beta-(1 -> 2), beta-(1 -> 5) linkages relevant to LAM were synthesized through chemical glycosylations. The efficacies of synthetic glycolipids to interact with SP-A were assessed by using the surface plasmon resonance (SPR) technique, from which association-dissociation rate constants and equilibrium binding constants were derived. The equilibrium binding constants of the interaction of two constitutionally varying beta-arabinofuranoside glycolipids with SP-A were found to be in the millimolar range. A comparison of the results with few alpha-anomeric arabinofuranoside glycolipids showed that glycolipids with beta-anomeric linkages were having relatively lower equilibrium binding constants than those with alpha-anomeric linkages in binding to the protein, whereas oligosaccharides alone, without lipidic chains, exhibited higher equilibrium binding constants. Further, the synthetic compounds inhibited the growth of mycobacteria and affected sliding motilities of the bacteria, although to an extent relatively lesser than that of synthetic compounds constituted with alpha-anomeric linkages.

Item Type:	Journal Article
Publication:	Glycoconjugate Journal
Publisher:	Springer
Additional Information:	Copyright of this article belongs to Springer.
Keywords:	beta-Arabinofuranosides;Glycolipids;Glycosylation;M. smegmatis;Sliding motility;Surface plasmon resonance; Surfactant protein-A
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit Division of Chemical Sciences > Organic Chemistry
Date Deposited:	01 May 2012 10:21
Last Modified:	01 May 2012 10:21
URI:	http://eprints.iisc.ac.in/id/eprint/44339

Actions (login required)

View Item