Binding region and interaction properties of sulfoquinovosylacylglycerol (SQAG) with human vascular endothelial growth factor 165 revealed by biosensor-based assays
MedChemComm, ISSN: 2040-2503, Vol: 2, Issue: 12, Page: 1188-1193
2011
- 7Citations
- 6Captures
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Article Description
Sulfoquinovosylacylglycerol (SQAG) is a sulfoglycolipid showing anti-angiogenic and radiosensitizing effects for treatment of solid tumors both in vitro and in vivo. Here we elucidated the interaction of SQAG with various growth factors and their cognate receptors for vascular formation using biosensor-based assays. The structure-binding relationship was also determined. Our results show that βSQDG selectively recognizes heparin binding domain (HBD) in human vascular endothelial growth factor 165 (hVEGF ) with an affinity in the order of 10 M. The presence of both a sulfate moiety and at least one C length fatty acid chain is essential for binding. Conversion of anomeric configurations in SQAG did not alter the affinity with hVEGF . This SQAG association inhibited T7 phage-displayed HBD binding to neuropilin-1 (NRP1), a VEGF receptor on the endothelial cell surface of blood vessels that specifically recognizes HBD in hVEGF . © 2011 The Royal Society of Chemistry.
Bibliographic Details
Royal Society of Chemistry (RSC)
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