Selective Binding of Endostatin Peptide 4 to Recombinant VEGF Receptor 3 In Vitro

Author(s): Kyu-Yeon Han, Michael Chang, Hong-Yu Ying, Hyun Lee, Yu-hui Huang, Jin-Hong Chang, Dimitri T. Azar.

Journal Name: Protein & Peptide Letters

Volume 22 , Issue 11 , 2015

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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 5.72x10-8 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.

Keywords: Collagen XVIII, endostatin, neostatin, VEGFR1, VEGFR2 and VEGFR3.

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Article Details

Year: 2015
Page: [1025 - 1030]
Pages: 6
DOI: 10.2174/0929866522666150907111953
Price: $65

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