Jump to main content
Jump to site search

Issue 26, 2017
Previous Article Next Article

Incorporation of ‘click’ chemistry glycomimetics dramatically alters triple-helix stability in an adiponectin model peptide

Author affiliations

Abstract

Adiponectin (Adpn) has been shown to be a possible therapeutic for Type II diabetes, however the production of a therapeutic version of Adpn has proved to be challenging. Biological studies have highlighted the importance of the glycosylated lysine residues for the formation of bioactive high molecular weight oligomers of Adpn. Through the use of ‘click’ glycopeptide mimetics, we investigated the role of glycosylated lysine and serine residues for the formation of triple helical structures of the collagenous domain of Adpn, in the context of a collagen model peptide scaffold. The physical properties of the unglycosylated lysine and serine peptides are compared with their glycosylated analogues. Our results highlight the crucial role of lysine residues for formation of the triple helical structure of Adpn, possibly due to the extension of both intra- and interstrand hydrogen bonding networks. Strikingly, we observed a significant decrease in thermal stability upon incorporation of triazole-linked analogues of glycosylated lysine residues into the adiponectin collageneous domain, indicating possible uses of ‘click’ glycomimetics for bioengineering applications.

Graphical abstract: Incorporation of ‘click’ chemistry glycomimetics dramatically alters triple-helix stability in an adiponectin model peptide

Back to tab navigation

Supplementary files

Publication details

The article was received on 08 Jun 2017, accepted on 16 Jun 2017 and first published on 16 Jun 2017


Article type: Paper
DOI: 10.1039/C7OB01388D
Citation: Org. Biomol. Chem., 2017,15, 5602-5608
  •   Request permissions

    Incorporation of ‘click’ chemistry glycomimetics dramatically alters triple-helix stability in an adiponectin model peptide

    K. R. Lutteroth, P. W. R. Harris, T. H. Wright, H. Kaur, K. Sparrow, S. Yang, G. J. S. Cooper and M. A. Brimble, Org. Biomol. Chem., 2017, 15, 5602
    DOI: 10.1039/C7OB01388D

Search articles by author

Spotlight

Advertisements