1. Academic Validation
  2. Effect of RGD-4C position is more important than disulfide bonds on antiangiogenic activity of RGD-4C modified endostatin derived synthetic polypeptide

Effect of RGD-4C position is more important than disulfide bonds on antiangiogenic activity of RGD-4C modified endostatin derived synthetic polypeptide

  • Bioconjug Chem. 2010 Jul 21;21(7):1142-7. doi: 10.1021/bc900292y.
Runting Yin 1 Heng Zheng Tao Xi Han-Mei Xu
Affiliations

Affiliation

  • 1 Department of Marine Pharmacy, College of Life Science and Technology, China Pharmaceutical University, Nanjing, 210009, P. R. China.
Abstract

ES-2 (IVRRADRAAVP), an endostatin-derived synthetic polypeptide, contains the Amino acids 50-60 of endostatin from its N terminus, and it had no inhibitory effects on tumor growth in vivo. In order to increase the targeted delivery of ES-2 to tumors and further enhance the activity, the polypeptide RGD-4C (ACDCRGDCFC) was introduced into ES-2, and the effects of RGD-4C position and RGD-4C disulfide bonds on polypeptides activity were investigated. When RGD-4C polypeptides (with or without disulfide bonds) were introduced to the N-terminals of synthesized ES-2, the modified ES-2 showed significant antitumor activity in vivo. Cell proliferation and chicken chorioallantoic membrane (CAM) assay results showed that disulfide bonds had no significant effects on RGD-4C-modified ES-2 antiangiogenic activity. Furthermore, the target of modified Peptides was Integrin alpha5beta1, rather than Integrin alphavbeta3 as previous studies mentioned.

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Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-P3732
    99.82%, αv-integrin Ligand