[Isolation and characterization of collagen-binding domains from human von Willebrand factor]

Mol Gen Mikrobiol Virusol. 2009:(3):31-5.
[Article in Russian]

Abstract

DNA fragments encoding for two collagen binding decapeptides from the human von Willebrand factor (vWF-H1 and vWF-H2) were cloned in the Escherichia coil culture. Overproducing strains of the chimeric proteins vWF(H1)-CBD and vWF(H2)-CBD consisting of the corresponding decapeptide, Gly-Ser spacer and a cellulose binding domain (CBD) from Anaerocellum thermophilum were constructed. Using one-stage purification on cellulose, the highly purified samples of vWF(H1)-CBD and vWF(H2)-CBD proteins were obtained and the ability of these proteins to bind collagen was studied. These constructions are planned to be used for development of the recombinant collagen binding proteins with different biological activities, which, in its turn, will be used for development of the new generation products and materials for medicine, such as different kinds of implants, the coats, etc.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • Collagen / chemistry
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Humans
  • Oligopeptides / genetics*
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • von Willebrand Factor / chemistry*
  • von Willebrand Factor / genetics

Substances

  • Oligopeptides
  • Recombinant Proteins
  • von Willebrand Factor
  • Collagen