Selective binding of endostatin peptide 4 to recombinant VEGF receptor 3 in vitro

We previously reported that neostatin,a proteolytic fragment of collagen xviii that includes endostatin,inhibits basic fibroblast growth factor-induced corneal angiogenesis and lymphangiogenesis. in experiments to determine which fragments in neostatin are responsible for binding to vegf receptors (vegfrs),we previously showed that a 28- mer sequence at the c-terminal of endostatin,known as endostatin peptide 9,preferentially binds vegfr3-fc over vegfr1-fc and vegfr2-fc. in the present study,we show that a different endostatin fragment,endostatin peptide 4 (26 mers long),also selectively binds vegfr3-fc and not vegfr1-fc or vegfr2-fc. from surface plasmon resonance data,the kd and chi2 (ru2) values for endostatin peptide 4 binding to vegfr3-fc are 5.72×10-8 m and 0.354,respectively. in conclusion,endostatin peptides 4 and 9 may be responsible for endostatin binding to vegfr3-fc,and this improved understanding of endostatin peptide binding to vegfr3-fc may support the development of therapeutics targeting lymphangiogenic processes. © 2015 bentham science publishers.