Probing the interactions of phosphosulfomannans with angiogenic growth factors by surface plasmon resonance
Probing the interactions of phosphosulfomannans with angiogenic growth factors by surface plasmon resonance
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DOI:
10.1021/jm030180y
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发表时间:
2003-10-09
影响因子:
7.3
通讯作者:
Ferro, V
中科院分区:
文献类型:
--
作者:
Cochran, S;Li, CP;Ferro, V
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 Mold 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.