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Protein Adsorption into Mesopores: A Combination of Electrostatic Interaction, Counterion Release and van der Waals Forces
Publikationstyp
Journal Article
Date Issued
2014-03-18
Sprache
English
Author(s)
TORE-URI
Volume
30
Issue
10
Start Page
2729
End Page
2737
Citation
Langmuir 30 (10): 2729-2737 (2014-03-18)
Publisher DOI
Scopus ID
PubMed ID
24571263
ArXiv ID
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, i.e. 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.
Subjects
Physics - Biological Physics
Physics - Biological Physics
Physics - Mesoscopic Systems and Quantum Hall Effect
Physics - Materials Science
Physics - Soft Condensed Matter
Physics - Chemical Physics