A 'clicked' tetrameric hydroxamic acid glycopeptidomimetic antagonizes sugar-lectin interactions on the cellular level

Hai-Lin Zhang; Yi Zang; Juan Xie; Jia Li; Guo-Rong Chen; Xiao-Peng He; He Tian

doi:10.1038/srep05513

A 'clicked' tetrameric hydroxamic acid glycopeptidomimetic antagonizes sugar-lectin interactions on the cellular level

Sci Rep. 2014 Jul 1:4:5513. doi: 10.1038/srep05513.

Authors

Hai-Lin Zhang¹, Yi Zang², Juan Xie³, Jia Li², Guo-Rong Chen¹, Xiao-Peng He¹, He Tian¹

Affiliations

¹ Key Laboratory for Advanced Materials & Institute of Fine Chemicals, East China University of Science and Technology, 130 Meilong Rd., Shanghai 200237, PR China.
² National Center for Drug Screening, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 189 Guo Shoujing Rd., Shanghai 201203, PR China.
³ PPSM, Institut d'Alembert, ENS de Cachan, CNRS UMR 8531, 61 Avenue du Pt Wilson, F-94235 Cachan, France.

Abstract

A tetrameric N-acetyl galactosaminyl (GalNAc) peptidomimetic was constructed by N-acetylation of repeating proline-based hydroxamic acid units, followed by a convergent 'click chemistry' coupling. This novel glycopeptidomimetic was determined to effectively antagonize the interaction between a transmembrane hepatic lectin and GalNAc on the cellular level.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

3T3 Cells
Animals
Biomimetic Materials / administration & dosage
Biomimetic Materials / chemical synthesis
Carbohydrate Metabolism / drug effects
Carbohydrate Metabolism / physiology*
Click Chemistry / methods
Dose-Response Relationship, Drug
Glycopeptides / chemistry
Hep G2 Cells
Humans
Hydroxamic Acids / administration & dosage*
Hydroxamic Acids / chemistry*
Lectins / metabolism*
Mice
Peptides / administration & dosage*
Peptides / chemistry*

Substances

Glycopeptides
Hydroxamic Acids
Lectins
Peptides