Advertisement

 

 

Site-Selective Chemoenzymatic Glycosylation of an HIV-1 Polypeptide Antigen with Two Distinct N-Glycans via an Orthogonal Protecting Group Strategy.

Site-Selective Chemoenzymatic Glycosylation of an HIV-1 Polypeptide Antigen with Two Distinct N-Glycans via an Orthogonal Protecting Group Strategy.
Author Information (click to view)

Toonstra C, Amin MN, Wang LX,


Toonstra C, Amin MN, Wang LX, (click to view)

Toonstra C, Amin MN, Wang LX,

Advertisement
Share on FacebookTweet about this on TwitterShare on LinkedIn

The Journal of organic chemistry 2016 07 0781(15) 6176-85 doi 10.1021/acs.joc.6b01044

Abstract

A convergent chemoenzymatic approach for sequential installation of different N-glycans in a polypeptide is described. The method includes introduction of distinguishably protected GlcNAc-Asn building blocks during automated solid phase peptide synthesis (SPPS), followed by orthogonal deprotection of the GlcNAc primers and site-selective sequential extension of the sugar chains through glycosynthase-catalyzed transglycosylation reactions. It was observed that the protecting groups on one neighboring GlcNAc moiety have an impact on the substrate activity of another GlcNAc acceptor toward some endoglycosynthases in transglycosylation. The usefulness of this synthetic strategy was exemplified by an efficient synthesis of the glycopeptide neutralizing epitope of broadly HIV-neutralizing antibody PG9. The method should be generally applicable for the synthesis of complex glycopeptides carrying multiple different N-glycans.

Submit a Comment

Your email address will not be published. Required fields are marked *

2 × one =

[ HIDE/SHOW ]