Heparin-Induced Changes of Vascular Endothelial Growth Factor (VEGF₁₆₅) Structure.

ABSTRACT: Vascular endothelial growth factor-A (VEGF-A), a secreted homodimeric glycoprotein, is a critical regulator of angiogenesis in normal and pathological states. The binding of heparin (HE) to VEGF₁₆₅ (the major form of VEGF-A) modulates the angiogenesis-related cascade, but the mechanism of the observed changes at the structural level is still insufficiently explored. In the present study, we examined the effect of HE on the structural and physicochemical properties of recombinant human VEGF₁₆₅ (rhVEGF₁₆₅). The HE binding results in an increase of hydrophobic surface exposure in rhVEGF₁₆₅ without changes in its secondary structure. Differential scanning calorimetry measurements for intact and HE-bound rhVEGF₁₆₅ reveals the absence of any

SUBMITTER: Nemashkalova EL 

PROVIDER: S-EPMC9856036 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature