Presentation of fibronectin fragments using affinity protein interactions for enhanced retention and function

Acta Biomater. 2014 Dec;10(12):4956-4960. doi: 10.1016/j.actbio.2014.08.026. Epub 2014 Aug 27.

Abstract

We present a protein immobilization system, based on the Src Homology 3 (SH3) affinity domain, allowing for a transient interaction between a fibronectin ligand and a biomaterial surface. This strategy leads to enhanced retention of the fibronectin fragment over adsorbed fibronectin, and increased cellular proliferation and motility over either covalently immobilized or adsorbed fibronectin. The results indicate that intermediate affinity protein immobilization could provide benefits for tissue engineering beyond the traditional immobilization techniques, adsorption or covalent attachment.

Keywords: Affinity; Cell motility; Engineered proteins; Fibronectin; Wound healing.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry*
  • Adsorption
  • Animals
  • Binding Sites
  • Cell Movement / physiology*
  • Cell Proliferation / physiology*
  • Coated Materials, Biocompatible / chemical synthesis*
  • Fibronectins / chemistry*
  • Materials Testing
  • Mice
  • NIH 3T3 Cells
  • Phosphoproteins / chemistry*
  • Protein Binding
  • Tissue Engineering / methods*
  • src Homology Domains*

Substances

  • Adaptor Proteins, Signal Transducing
  • Coated Materials, Biocompatible
  • Fibronectins
  • Phosphoproteins
  • SLP-76 signal Transducing adaptor proteins