Expression and characterization of recombinant NH2-terminal cell binding fragment of vitronectin in E. coli

Biotechnol Lett. 2003 Dec;25(23):1973-5. doi: 10.1023/b:bile.0000004387.96353.21.

Abstract

A recombinant peptide fragment of vitronectin (rVN143), that includes the Arg-Gly-Asp (RGD) cell recognition site, was expressed in Escherichia coli using a prokaryotic expression system. The addition of recombinant rVN143 peptide enhances cell adhesion and proliferation similar (approximately 70%) to those of native VN.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Biomimetic Materials / metabolism*
  • Cell Adhesion / drug effects
  • Cell Adhesion / physiology
  • Cell Division / drug effects
  • Cell Division / physiology
  • Cloning, Molecular
  • Dose-Response Relationship, Drug
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Fibroblasts / cytology
  • Fibroblasts / drug effects*
  • Fibroblasts / physiology*
  • Gene Expression Regulation, Bacterial / physiology
  • Gingiva / metabolism
  • Humans
  • Peptide Fragments / biosynthesis
  • Peptide Fragments / chemistry
  • Protein Binding
  • Protein Engineering / methods*
  • Structure-Activity Relationship
  • Vitronectin / biosynthesis*
  • Vitronectin / classification
  • Vitronectin / pharmacology*

Substances

  • Peptide Fragments
  • Vitronectin