Abstract
C-phycocyanin (C-PC) produced from cyanobacterial species finds application in drug development. Therefore, it is of interest to document the molecular binding features of C-PC with the vascular endothelial growth factor receptor 2 (VEGFR2). C-PC showed H-bond interactions with residues on both sides of the Deusche Forschugsgemein-Schalt (DFG) loop (Asp1046-Phe1047-Gly1048). A hydrophobic association between the activation loop and the DFG residue (Gly1048) helps to inhibit the activity of VEGFR2 kinases. Thus, C-PC is reported as a potential angiogenesis inhibitor for VEGFR2 in combating cancer.