Biswas, Margaret and Rao, VSR (1980) Conformational analysis of the milk oligosaccharides. In: Biopolymers, 19 (8). pp. 1555-1566.
|
PDF
page98.pdf Download (554kB) |
Abstract
Possible conformations of lacto-N-tetraose, lacto-N-neotetraose, related disaccharides, and other milk oligosaccharides have been studied by an energy-minimization procedure using empirical potential functions. Lacto-N-tetraose favors a "curved" conformation, while lacto-N-neotetraose favors an approximately "straight" conformation. These two conformations differ mainly in the position of the terminal galactose residue with respect to the rest of the molecule. This difference explains the greater strength of lacto-N-neotetraose compared with lacto-N-tetraose in its ability to inhibit the cross-reaction of blood group P1 fractions with Type XIV pneumococcal antipolysaccharide. Although the favored conformation of lacto-N-tetraose (inactive) agrees with the model proposed by the earlier workers, that for lacto-N-neotetraose (active) differs. The favored conformations for the disaccharides galactose- \beta (1-4)-N-acetylglucosamine, galactose-\beta (1-3)-N-acetylglucosamine, and lactose are similar in overall shape, differing only in the nature and orientation of the side groups. This explains their nearly equal inhibitory activity. These theoretical models also explain the increased activity of lacto-N-fucopentaose I over that of lacto-N-tetraose and the relative activities of the substituted lactoses. The present studies suggest that it is the overall shape of the molecule which is important for activity, rather than the terminal \beta (1-4)-linked galactose residue alone.
Item Type: | Journal Article |
---|---|
Publication: | Biopolymers |
Publisher: | John Wiley & Sons, Inc. |
Additional Information: | The copyright belongs to John Wiley & Sons, Inc. |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 07 Aug 2008 |
Last Modified: | 19 Sep 2010 04:21 |
URI: | http://eprints.iisc.ac.in/id/eprint/4279 |
Actions (login required)
View Item |