Effects of protein solution composition on the time-dependent functional activity of fibrinogen on surfaces

Pranav Soman, Christopher A. Siedlecki

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Protein function affects subsequent biological processes such as cell adhesion and thrombus formation. We have developed tools to detect the biological activity of fibrinogen using AFM techniques. In this work, we measure the effects of solution concentration, residence time, and protein competition with BSA on the time-dependent functional changes in adsorbed fibrinogen on mica surface. AFM probes were functionalized with monoclonal antibodies recognizing fibrinogen gamma 392-411, which includes the platelet binding dodecapeptide region. Results show good correlation between changes in biological activity of adsorbed fibrinogen at the molecular scale measured by AFM and platelet adhesion measured at a macroscale. Furthermore, the results show that inclusion of BSA into the solution moves the peak biological activity of fibrinogen to earlier time points. These results illustrate a complex and dynamic biological interface and offer new opportunities for improved insights into the molecular basis for the biological response to biomaterials.

Original languageEnglish (US)
Pages (from-to)10814-10819
Number of pages6
JournalLangmuir
Volume27
Issue number17
DOIs
StatePublished - Sep 6 2011
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • Electrochemistry
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Materials Science(all)
  • Spectroscopy

Cite this