Next Article in Journal
Transcriptome Analysis of Kiwifruit in Response to Pseudomonas syringae pv. actinidiae Infection
Next Article in Special Issue
Galectin-3: One Molecule for an Alphabet of Diseases, from A to Z
Previous Article in Journal
Frame-Insensitive Expression Cloning of Fluorescent Protein from Scolionema suvaense
Previous Article in Special Issue
Overall Survival of Ovarian Cancer Patients Is Determined by Expression of Galectins-8 and -9
Article Menu
Issue 2 (February) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2018, 19(2), 372; doi:10.3390/ijms19020372

Poly-N-Acetyllactosamine Neo-Glycoproteins as Nanomolar Ligands of Human Galectin-3: Binding Kinetics and Modeling

1
Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 14220 Prague, Czech Republic
2
Laboratory for Biomaterials, Institute for Biotechnology and Helmholtz-Institute for Biomedical Engineering, RWTH Aachen University, Pauwelsstrasse 20, 52074 Aachen, Germany
3
Department of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Technická 3, 16628 Prague 6, Czech Republic
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Received: 15 January 2018 / Revised: 22 January 2018 / Accepted: 23 January 2018 / Published: 26 January 2018
(This article belongs to the Special Issue Galectins in Cancer and Translational Medicine)
View Full-Text   |   Download PDF [4003 KB, uploaded 26 January 2018]   |  

Abstract

Galectin-3 (Gal-3) is recognized as a prognostic marker in several cancer types. Its involvement in tumor development and proliferation makes this lectin a promising target for early cancer diagnosis and anti-cancer therapies. Gal-3 recognizes poly-N-acetyllactosamine (LacNAc)-based carbohydrate motifs of glycoproteins and glycolipids with a high specificity for internal LacNAc epitopes. This study analyzes the mode and kinetics of binding of Gal-3 to a series of multivalent neo-glycoproteins presenting complex poly-LacNAc-based oligosaccharide ligands on a scaffold of bovine serum albumin. These neo-glycoproteins rank among the strongest Gal-3 ligands reported, with Kd reaching sub-nanomolar values as determined by surface plasmon resonance. Significant differences in the binding kinetics were observed within the ligand series, showing the tetrasaccharide capped with N,N′-diacetyllactosamine (LacdiNAc) as the strongest ligand of Gal-3 in this study. A molecular model of the Gal-3 carbohydrate recognition domain with docked oligosaccharide ligands is presented that shows the relations in the binding site at the molecular level. The neo-glycoproteins presented herein may be applied for selective recognition of Gal-3 both on the cell surface and in blood serum. View Full-Text
Keywords: carbohydrate; galectin-3; galectins in diagnosis; galectins in therapy; glycosyltransferase; surface plasmon resonance; molecular modeling carbohydrate; galectin-3; galectins in diagnosis; galectins in therapy; glycosyltransferase; surface plasmon resonance; molecular modeling
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Bumba, L.; Laaf, D.; Spiwok, V.; Elling, L.; Křen, V.; Bojarová, P. Poly-N-Acetyllactosamine Neo-Glycoproteins as Nanomolar Ligands of Human Galectin-3: Binding Kinetics and Modeling. Int. J. Mol. Sci. 2018, 19, 372.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top