Retro-inverso carbohydrate mimetic peptides with annexin1-binding selectivity, are stable in vivo, and target tumor vasculature

PLoS One. 2013 Dec 2;8(12):e80390. doi: 10.1371/journal.pone.0080390. eCollection 2013.

Abstract

Previous research suggests that carbohydrate mimetic peptide IF7 (IFLLWQR) has an excellent targeting property to annexin1 (Anxa1), a specific marker on the tumor endothelium. However, IF7 is susceptible to proteolysis and has a poor stability in vivo. We prepared a D-amino acid, reverse sequence peptide of IF7, designated RIF7, to confer protease resistance while retaining bioactivity. Experimental results indicate that RIF7 had significantly increased stability and an increased receptor binding affinity than IF7, and this new moiety may represent a clinically relevant vehicle for anticancer drugs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiogenesis Inhibitors / chemistry
  • Angiogenesis Inhibitors / pharmacology*
  • Animals
  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / pharmacology*
  • Biomimetic Materials / chemistry
  • Biomimetic Materials / pharmacology*
  • Cell Line, Tumor
  • Humans
  • Male
  • Mice
  • Mice, Inbred BALB C
  • Mice, Nude
  • Neoplasms, Experimental / blood supply
  • Neoplasms, Experimental / drug therapy
  • Neoplasms, Experimental / pathology
  • Neovascularization, Pathologic* / drug therapy
  • Neovascularization, Pathologic* / pathology
  • Peptides / chemistry
  • Peptides / pharmacology*

Substances

  • Angiogenesis Inhibitors
  • Antineoplastic Agents
  • Peptides

Grants and funding

The work was sponsored by National Nature Science Foundation of China (81273459), Shanghai Rising-Star Program (10QA1400800), National Basic Research Program of China (2013CB932500) and National Science and Technology Major Project (2012ZX09304004). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.