Protein spreading kinetics at liquid-solid interfaces via an adsorption probe method
We report the areal growth kinetics of fibrinogen adsorbed on model hydrophobic and hydrophilic surfaces measured via an adsorption probe method. This approach exploits the adsorption of probe molecules to determine the evolution of fibrinogen test molecules under conditions where the fibrinogen tes...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 21(2005), 22 vom: 25. Okt., Seite 10172-8 |
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| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2005
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, U.S. Gov't, Non-P.H.S. Proteins Fibrinogen 9001-32-5 Muramidase EC 3.2.1.17 |
| Zusammenfassung: | We report the areal growth kinetics of fibrinogen adsorbed on model hydrophobic and hydrophilic surfaces measured via an adsorption probe method. This approach exploits the adsorption of probe molecules to determine the evolution of fibrinogen test molecules under conditions where the fibrinogen test molecules adsorb at relatively dilute surface conditions, minimizing interactions between them. It is found that fibrinogen test molecules spread from an average initial footprint of 100 nm2 to a final footprint near 500 nm2 per molecule on the hydrophobic surface, with a single-exponential decay of 1735 s. On a hydrophilic monolayer, the area increases from 100 to 160 nm2 with a characteristic time of 6740 s. These results demonstrate the power of the adsorption probe approach and comprise the first measurements of the averaged area relaxations of adsorbed proteins. The observation of single-exponential dynamics is remarkable, given the extensive relaxation on the hydrophobic surface, which must involve fibrinogen denaturing |
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| Beschreibung: | Date Completed 04.06.2007 Date Revised 18.10.2005 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |