Probing the interactions of phosphosulfomannans with angiogenic growth factors by surface plasmon resonance

Cochran, S., Li, C., Fairweather, J.K., Kett, W.C., Coombe, D.R. and Ferro, V. (2003) Probing the interactions of phosphosulfomannans with angiogenic growth factors by surface plasmon resonance. Journal of Medicinal Chemistry, 46 21: 4601-4608. doi:10.1021/jm030180y


Author Cochran, S.
Li, C.
Fairweather, J.K.
Kett, W.C.
Coombe, D.R.
Ferro, V.
Title Probing the interactions of phosphosulfomannans with angiogenic growth factors by surface plasmon resonance
Journal name Journal of Medicinal Chemistry   Check publisher's open access policy
ISSN 0022-2623
1520-4804
Publication date 2003-09-09
Sub-type Article (original research)
DOI 10.1021/jm030180y
Volume 46
Issue 21
Start page 4601
End page 4608
Total pages 8
Editor Philip S. Portoghese
Laurence H. Hurley
Yusuf J. Abul-Hajj
Place of publication Washington, D.C., U.S.A.
Publisher American Chemical Society
Language eng
Subject 0304 Medicinal and Biomolecular Chemistry
1115 Pharmacology and Pharmaceutical Sciences
Formatted abstract
The binding interactions of the phosphosulfomannan anticancer agent PI-88 (1) with the angiogenic growth factors FGF-1, FGF-2, and VEGF were studied by surface plasmon resonance (SPR) on a BIAcore 3000 biosensor. Compared with heparin, PI-88 has at least 11-fold higher affinity for FGF-1 and at least 3-fold higher affinity for VEGF, but at least 13-fold lower affinity for FGF-2. To define the structural features of PI-88 that are important for growth factor binding, several analogues, such as dephosphorylated PI-88 and a sulfated pentasaccharide, were prepared. The binding interactions of these analogues with FGF-1, FGF-2, and VEGF were similarly studied by SPR, and structure-activity relationships were determined.
Copyright © 2003 American Chemical Society.

Keyword Angiogenic factor
Antineoplastic agent
Fibroblast growth factor 2
Pi 88
Protein interaction
Heparin
Phosphosulfomannans
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 62 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 64 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 30 Mar 2010, 12:43:48 EST by June Temby on behalf of Faculty of Science