Kinetics of fibrinogen adsorption on hydrophilic substrate

2010
journal article
article
63
dc.abstract.enIrreversible 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.affiliationWydział Fizyki, Astronomii i Informatyki Stosowanej : Instytut Fizyki im. Mariana Smoluchowskiegopl
dc.contributor.authorAdamczyk, Zbigniewpl
dc.contributor.authorBarbasz, Jakub - 160063 pl
dc.contributor.authorCieśla, Michał - 101020 pl
dc.date.accessioned2015-11-13T08:20:08Z
dc.date.available2015-11-13T08:20:08Z
dc.date.issued2010pl
dc.description.number14pl
dc.description.physical11934-11945pl
dc.description.volume26pl
dc.identifier.doi10.1021/la101261fpl
dc.identifier.eissn1520-5827pl
dc.identifier.issn0743-7463pl
dc.identifier.urihttp://ruj.uj.edu.pl/xmlui/handle/item/16727
dc.languageengpl
dc.language.containerengpl
dc.rightsDodaję tylko opis bibliograficzny*
dc.rights.licencebez licencji
dc.rights.uri*
dc.subject.enadsorptionpl
dc.subject.enmolecularpl
dc.subject.enfibrinogenpl
dc.subject.enprotein conformationpl
dc.subject.enmodelspl
dc.subject.enkineticspl
dc.subject.enfibrinogen: chemistrypl
dc.subject.enhydrophobic and hydrophilic iInteractionspl
dc.subject.ensurface propertiespl
dc.subtypeArticlepl
dc.titleKinetics of fibrinogen adsorption on hydrophilic substratepl
dc.title.journalLangmuirpl
dc.typeJournalArticlepl
dspace.entity.typePublication
dc.abstract.enpl
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.
dc.affiliationpl
Wydział Fizyki, Astronomii i Informatyki Stosowanej : Instytut Fizyki im. Mariana Smoluchowskiego
dc.contributor.authorpl
Adamczyk, Zbigniew
dc.contributor.authorpl
Barbasz, Jakub - 160063
dc.contributor.authorpl
Cieśla, Michał - 101020
dc.date.accessioned
2015-11-13T08:20:08Z
dc.date.available
2015-11-13T08:20:08Z
dc.date.issuedpl
2010
dc.description.numberpl
14
dc.description.physicalpl
11934-11945
dc.description.volumepl
26
dc.identifier.doipl
10.1021/la101261f
dc.identifier.eissnpl
1520-5827
dc.identifier.issnpl
0743-7463
dc.identifier.uri
http://ruj.uj.edu.pl/xmlui/handle/item/16727
dc.languagepl
eng
dc.language.containerpl
eng
dc.rights*
Dodaję tylko opis bibliograficzny
dc.rights.licence
bez licencji
dc.rights.uri*
dc.subject.enpl
adsorption
dc.subject.enpl
molecular
dc.subject.enpl
fibrinogen
dc.subject.enpl
protein conformation
dc.subject.enpl
models
dc.subject.enpl
kinetics
dc.subject.enpl
fibrinogen: chemistry
dc.subject.enpl
hydrophobic and hydrophilic iInteractions
dc.subject.enpl
surface properties
dc.subtypepl
Article
dc.titlepl
Kinetics of fibrinogen adsorption on hydrophilic substrate
dc.title.journalpl
Langmuir
dc.typepl
JournalArticle
dspace.entity.type
Publication

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