Complete unfolding of fibronectin reveals surface interactions

Lynn Donlon, Darman Nordin, Daniel Frankel

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Surface interactions between proteins and biomaterials are fundamental to biological processes and a means to measure these interactions with minimum perturbation to the system of interest has remained elusive. In this paper we address this problem by analysing the total unfolding force of a surface adsorbed protein, in this case fibronectin. By summing all unfolding events, domains that may be interacting with the surface are considered. We propose a protocol for comparing like with like in terms of protein behaviour based on the number of events in the sawtooth pattern. Using this method it is possible to distinguish surface behaviour between several biologically relevant surfaces including hydroxyapatite, collagen and lipids. Moreover the difference in total unfolding confirms the difference in protein interaction/conformation on the various surfaces.

Original languageEnglish
Pages (from-to)9933-9940
Number of pages8
JournalSoft Matter
Volume8
Issue number38
DOIs
Publication statusPublished - 2012

Fingerprint

Fibronectins
surface reactions
proteins
Proteins
collagens
Biocompatible Materials
Durapatite
lipids
Conformations
interactions
Collagen
perturbation
Lipids

ASJC Scopus subject areas

  • Chemistry(all)
  • Condensed Matter Physics

Cite this

Complete unfolding of fibronectin reveals surface interactions. / Donlon, Lynn; Nordin, Darman; Frankel, Daniel.

In: Soft Matter, Vol. 8, No. 38, 2012, p. 9933-9940.

Research output: Contribution to journalArticle

Donlon, Lynn ; Nordin, Darman ; Frankel, Daniel. / Complete unfolding of fibronectin reveals surface interactions. In: Soft Matter. 2012 ; Vol. 8, No. 38. pp. 9933-9940.
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