4.8 Article

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

Journal

ACTA BIOMATERIALIA
Volume 10, Issue 12, Pages 4956-4960

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.actbio.2014.08.026

Keywords

Wound healing; Fibronectin; Engineered proteins; Affinity; Cell motility

Funding

  1. Air Products
  2. Georgia Tech
  3. NSF

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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. (C) 2014 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.

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