Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Twelve novel glycomethanethiosulfonate (glyco-MTS) protein glycosylation reagents have been prepared. Their use in a controlled site-selective glycosylation strategy that combines site-directed mutagenesis with chemical modification allows protein glycosylation with concomitant control of (i) site, (ii) carbohydrate, (iii) anomeric stereochemistry, (iv) sugar to protein spacer arm nature and (v) degree of glycan protection. The ability of these highly selective and yet reactive reagents has been illustrated by the introduction of D-glucosyl and N-Ac-D-glucosaminyl residues to both external and hindered internal sites in a model protein - the serine protease enzyme subtilisin Bacillus lentus (SBL) - using corresponding gluco-MTS 1 and N-Ac-glucosamine-MTS 2. Molecular modelling studies provide a rationale for the strikingly different effects of these reagents on the properties of the protein despite differing only in the nature of their C-2 substituents. Copyright (C) 2000 Elsevier Science Ltd.

Original publication

DOI

10.1016/S0957-4166(99)00497-8

Type

Journal article

Journal

Tetrahedron Asymmetry

Publication Date

28/01/2000

Volume

11

Pages

245 - 262