A surface plasmon resonance-based solution affinity assay for heparan sulfate-binding proteins

Cochran, S., Ping Li, C. and Ferro, V. (2009) A surface plasmon resonance-based solution affinity assay for heparan sulfate-binding proteins. Glycoconjugate Journal, 26 5: 577-587. doi:10.1007/s10719-008-9210-0


Author Cochran, S.
Ping Li, C.
Ferro, V.
Title A surface plasmon resonance-based solution affinity assay for heparan sulfate-binding proteins
Journal name Glycoconjugate Journal   Check publisher's open access policy
ISSN 0282-0080
Publication date 2009-07
Sub-type Article (original research)
DOI 10.1007/s10719-008-9210-0
Volume 26
Issue 5
Start page 577
End page 587
Total pages 11
Place of publication United States
Publisher Springer New York LLC
Language eng
Subject 06 Biological Sciences
03 Chemical Sciences
Abstract A surface plasmon resonance-based solution affinity assay is described for measuring the K d of binding of heparin/heparan sulfate-binding proteins with a variety of ligands. The assay involves the passage of a pre-equilibrated solution of protein and ligand over a sensor chip onto which heparin has been immobilised. Heparin sensor chips prepared by four different methods, including biotin–streptavidin affinity capture and direct covalent attachment to the chip surface, were successfully used in the assay and gave similar K d values. The assay is applicable to a wide variety of heparin/HS-binding proteins of diverse structure and function (e.g., FGF-1, FGF-2, VEGF, IL-8, MCP-2, ATIII, PF4) and to ligands of varying molecular weight and degree of sulfation (e.g., heparin, PI-88, sucrose octasulfate, naphthalene trisulfonate) and is thus well suited for the rapid screening of ligands in drug discovery applications.
Keyword Heparan sulfate-binding proteins
heparin
solution affinity assay
surface plasmon resonance
Q-Index Code C1
Q-Index Status Provisional Code

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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Created: Wed, 29 Sep 2010, 16:19:12 EST by Laura McTaggart on behalf of Faculty of Science