| Literature DB >> 14521421 |
Siska Cochran1, Caiping Li, Jon K Fairweather, Warren C Kett, Deirdre R Coombe, Vito Ferro.
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.Entities:
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Year: 2003 PMID： 14521421 DOI： 10.1021/jm030180y
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446