Adhesion of α5β1 receptors to biomimetic substrates constructed from peptide amphiphiles

Angela K. Dillow, Sarah E. Ochsenhirt, James B. McCarthy, Gregg B. Fields, Matthew Tirrell

Research output: Contribution to journalArticlepeer-review

66 Scopus citations


Biomimetic membrane surfaces functionalized with fragments of the extracellular matrix protein, fibronectin, are constructed from mixtures of peptide and polyethylene glycol (PEG) amphiphiles. Peptides from the primary binding loop, GRGDSP, were used in conjunction with the synergy site peptide, PHSRN, in the III9-10 sites of human fibronectin. These peptides were attached to dialkyl lipid tails to form peptide amphiphiles. PEG amphiphiles were mixed in the layer to minimize non-specific adhesion in the background. GRGDSP and PEG amphiphiles or GRGDSP, PHSRN, and PEG amphiphiles were mixed in various ratios and deposited on solid substrates from the air-water interface using Langmuir-Blodgett techniques. In this method, peptide composition, density, and presentation could be controlled accurately. The effectiveness of these substrates to mimic native fibronectin is evaluated by their ability to generate adhesive forces when they are in contact with purified activated α5β1 integrin receptors that are immobilized on an opposing surface. Adhesion is measured using a contact mechanical approach (JKR experiment). The effects of membrane composition, density, temperature, and peptide conformation on adhesion to activated integrins in this simulated cell adhesion setup were determined. Addition of the synergy site, PHSRN, was found to increase adhesion of α5β1 to biomimetic substrates markedly. Increased peptide mobility (due to increased experimental temperature) increased integrin adhesion markedly at low peptide concentrations. A balance between peptide density and steric accessibility of the receptor binding face to α5β1 integrin was required for highest adhesion.

Original languageEnglish (US)
Pages (from-to)1493-1505
Number of pages13
Issue number12
StatePublished - Jun 15 2001

Bibliographical note

Funding Information:
The partial support of the National Institute of Health for this work through grant NIH-HL62427-01 is gratefully acknowledged. Support from the University of Minnesota Materials Research Science and Engineering Center is also acknowledged with appreciation.


  • Adhesion
  • Biomimetic materials
  • Peptides
  • RGD
  • Surface modification


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