4.8 Article

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

期刊

ACTA BIOMATERIALIA
卷 10, 期 12, 页码 4956-4960

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

关键词

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

资金

  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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