Investigating the effect of VEGF glycosylation on glycosaminoglycan binding and protein unfolding

VEGF(165) binding to endothelial cells is potentiated by glycosaminoglycans (GAGs). Here, we have investigated the impact of VEGF(165) N-glycosylation on GAG binding. Although glycosylated VEGF(165) bound to heparin with only slightly higher affinity than non-glycosylated VEGF(165), the natural ligand heparan sulfate induced a conformational change only in the glycosylated protein. Unfolding studies of the VEGF proteins indicated a stabilising effect of heparin on the growth factor structure. (c) 2005 Elsevier Inc. All rights reserved.