Issue 8, 2005

Functionalized foldamers: synthesis and characterization of a glycosylated β-peptide 314-helix conveying the TN-antigen

Abstract

Herein we describe the design, synthesis, and solution structure of a novel type of conjugate composed of a naturally occurring bio-active ligand bound to an artificial peptidomimetic backbone; in this first report on such functionalized foldamers we utilized a β-peptide as backbone and a GalNAc carbohydrate residue as ligand.

Graphical abstract: Functionalized foldamers: synthesis and characterization of a glycosylated β-peptide 314-helix conveying the TN-antigen

Supplementary files

Article information

Article type
Communication
Submitted
03 Mar 2005
Accepted
04 Mar 2005
First published
16 Mar 2005

Org. Biomol. Chem., 2005,3, 1359-1361

Functionalized foldamers: synthesis and characterization of a glycosylated β-peptide 314-helix conveying the TN-antigen

A. S. Norgren and P. I. Arvidsson, Org. Biomol. Chem., 2005, 3, 1359 DOI: 10.1039/B503237G

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements