Protein adsorption into mesopores : a combination of electrostatic interaction, counterion release, and van der Waals forces
Bovine heart cytochrome c has been immobilized into the mesoporous silica host material SBA-15 in both its native folded and urea-unfolded state. The comparison of the two folding states' behavior casts doubt on the commonly used explanation of cytochrome c adsorption, that is, the electrostati...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 30(2014), 10 vom: 18. März, Seite 2729-37 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
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2014
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Proteins SBA-15 Silicon Dioxide 7631-86-9 Cytochromes c 9007-43-6 |
| Zusammenfassung: | Bovine heart cytochrome c has been immobilized into the mesoporous silica host material SBA-15 in both its native folded and urea-unfolded state. The comparison of the two folding states' behavior casts doubt on the commonly used explanation of cytochrome c adsorption, that is, the electrostatic interaction model. A detailed investigation of the protein binding as a function of pH and ionic strength of the buffer solution reveals the complex nature of the protein-silica interaction. Electrostatic interaction, van der Waals forces, and entropic contributions by counterion release each contribute to adsorption on the silica pore walls |
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| Beschreibung: | Date Completed 14.11.2014 Date Revised 19.03.2014 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la404947j |