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Kinetics of fibrinogen adsorption on hydrophilic substrate


Kinetics of fibrinogen adsorption on hydrophilic substrate

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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 2015-11-13T08:20:08Z
dc.date.available 2015-11-13T08:20:08Z
dc.date.issued 2010 pl
dc.identifier.issn 0743-7463 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/16727
dc.language eng pl
dc.rights Dodaję tylko opis bibliograficzny *
dc.rights.uri *
dc.title Kinetics of fibrinogen adsorption on hydrophilic substrate pl
dc.type JournalArticle pl
dc.description.physical 11934-11945 pl
dc.abstract.en Irreversible side-on adsorption of fibrinogen, modeled as a linear chain of touching beads of various size, was studied theoretically using the random sequential adsorption (RSA) model. Numerical simulation of the Monte Carlo type enabled one to determine the dependence of the surface blocking function (available surface function) on the protein coverage. These numerical results were interpolated using analytical functions based on a polynomial expansion. The dependence of the jamming coverage on the size of the simulation area was also determined. By an extrapolation of these results to the infinite area size, the maximum surface concentration of fibrinogen for the side-on adsorption was determined to be 2.26 x 10(3) microm(-2). This corresponds to a jamming coverage theta(infinity) of 0.29. It was shown that the blocking function can well be approximated in the limit of high coverage by the dependence C(theta(infinity) - theta)(4). Using this interpolating expression, the kinetics of fibrinogen adsorption under convection and diffusion transport conditions were evaluated for various bulk concentrations of the protein. These kinetic curves were derived by numerically solving the mass transport equation in the bulk with the blocking function used as a nonlinear boundary condition at the interface. It was shown that our theoretical results are in agreement with experimental kinetic data obtained by AFM, ellipsometry, and other techniques for hydrophilic surfaces in the limit of low bulk fibrinogen concentration. pl
dc.subject.en adsorption pl
dc.subject.en molecular pl
dc.subject.en fibrinogen pl
dc.subject.en protein conformation pl
dc.subject.en models pl
dc.subject.en kinetics pl
dc.subject.en fibrinogen: chemistry pl
dc.subject.en hydrophobic and hydrophilic iInteractions pl
dc.subject.en surface properties pl
dc.description.volume 26 pl
dc.description.number 14 pl
dc.identifier.doi 10.1021/la101261f 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 [2010 A]: 32

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