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Journal of Biochemistry Advance Access published online on May 21, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm109
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© 2007 The Japanese Biochemical Society

Identification of a novel peptide ligand of human vascular endothelia growth factor receptor 3 for targeted tumor diagnosis and therapy

Xin Qin1,2, Yi Wan1,2, Meng Li1,2, Xiaochang Xue1,2, Shouzhen Wu1,2, Cun Zhang1,2, Yanjie You1,2, Weihua Wang1,2, Changli Jiang1,2, Yan Liu1,2, Wenhua Zhu1,2, Yonggang Ran1,2, Zhen Zhang1,2, Wei Han1,2,* and Yingqi Zhang1,2,*

1. Biotechnology Center of The Fourth Military Medical University. 17 Changle West Road, 710032 Xi’an, People’s Republic of China
2. State Key Laboratory of Cancer Biology. 17 Changle West Road, 710032 Xi’an, People’s Republic of China

*Wei Han or Yingqi Zhang, Biotechnology Center of The Fourth Military Medical University, 17 Changle West Road, 710032 Xi’an, P. R. China. Phone: +86-2983374775, Fax: +86-2983247213, E-mail: hanwwcn{at}yahoo.com.cn, or zhangyqh{at}fmmu.edu.cn

Received April 11, 2007; Accepted April 30, 2007


  Abstract

Human vascular endothelia growth factor receptor 3 (VEGFR-3) is upregulated in a variety of human cancers. It is a potentially rational target for drug delivery. To identify novel ligands with specific binding capabilities to VEGFR-3, we screened a phage display peptide library and found a consensus motif of the peptides which is displayed by the positive phages CSDxxHxWC (x is any amino acid). The phage displaying peptide CSDSWHYWC (designated as P1) exhibited the highest affinity to VEGFR-3 in phage ELISA and the chemically synthesized P1 could bind to VEGFR-3 specifically in a dose dependent manner. In addition, the flow cytometry assay and immunoflorenscence showed that the FITC labeled P1 could bind to VEGFR-3 positive carcinoma cells with specificity. Our study suggests that P1 may be a homing peptide for treatment of tumors.

Key Words: VEGFR-3, phage display, peptide


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