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Mechanisms of fibrinogen adsorption at solid substrates

Mechanisms of fibrinogen adsorption at solid substrates

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dc.contributor.author Adamczyk, Zbigniew pl
dc.contributor.author Barbasz, Jakub [SAP11019396] pl
dc.contributor.author Cieśla, Michał [SAP11018214] pl
dc.date.accessioned 2015-11-20T14:43:15Z
dc.date.available 2015-11-20T14:43:15Z
dc.date.issued 2011 pl
dc.identifier.issn 0743-7463 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/16994
dc.language eng pl
dc.rights Dodaję tylko opis bibliograficzny *
dc.rights.uri *
dc.title Mechanisms of fibrinogen adsorption at solid substrates pl
dc.type JournalArticle pl
dc.description.physical 6868-6878 pl
dc.abstract.other Adsorption of fibrinogen, modeled as a linear chain of touching beads of various sizes, was theoretically studied using the random sequential adsorption (RSA) model. The adsorption process was assumed to consist of two steps: (i) formation of an irreversibly bound fibrinogen monolayer under the side-on orientation, which is independent of the bulk protein concentration and (ii) formation of the reversibly bound, end-on monolayer, whose coverage was dependent on the bulk concentration. Calculation based on the RSA model showed that the maximum surface concentration of the end-on (reversible) monolayer equals N_{\perp \infty} = 6.13 \times 10^3 \mu m^{-2} which is much larger than the previously found value for the side-on (irreversible) monolayer, equal to N_{\infty} = 2.27 \times 10^3 \mu m^{-2}. Hence, the maximum surface concentration of fibrinogen in both orientations is determined to be 8.40 \times 10^3 \mu m^{-2} corresponding to the protein coverage of 5.70 mg m^{-2} assuming 20\% hydration. Additionally, the surface blocking function (ASF) was determined for the end-on fibrinogen adsorption, approximated for the entire range of coverage by the interpolating polynomial. For the coverage approaching the jamming limit, the surface blocking function (ASF) was shown to vanish proportionally to (\theta_{\perp \infty} - \theta_{\perp})^2. These calculation allowed one to theoretically predict adsorption isotherms for the end-on regime of fibrinogen and adsorption kinetics under various transport conditions (diffusion and convection). Using these theoretical results, a quantitative interpretation of experimental data obtained by TIRF and ellipsometry was successfully performed. The equilibriumadsorption constant for the end-on adsorption regime was found to be 8.04 \times 10^3 m. On the basis of this value, the depth of the adsorption energy minimum, equal to -17.4 kT, was predicted, which corresponds to \Delta G=-41.8 kJ mol^{-1}. This is in accordance with adsorption energy derived as the sum of the van der Waals and electrostatic interactions. Besides having significance for predicting fibrinogen adsorption, theoretical results derived in this work also have implications for basic science providing information on mechanisms of anisotropic protein molecule adsorption on heterogeneous surfaces. pl
dc.description.volume 27 pl
dc.description.number 11 pl
dc.identifier.doi 10.1021/la200798d pl
dc.identifier.eissn 1520-5827 pl
dc.title.journal Langmuir pl
dc.language.container eng pl
dc.affiliation Wydział Fizyki, Astronomii i Informatyki Stosowanej : Instytut Fizyki im. Mariana Smoluchowskiego pl
dc.subtype Article pl
dc.rights.original bez licencji pl
.pointsMNiSW [2011 A]: 35

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