Publisher DOI: 10.1021/acs.jpcc.5b09606
Title: PH-Dependent Selective Protein Adsorption into Mesoporous Silica
Language: English
Authors: Moerz, Sebastian T. 
Huber, Patrick 
Issue Date: 3-Dec-2015
Source: Journal of Physical Chemistry C 48 (119): 27072-79 (2015-12-03)
Journal or Series Name: The Journal of Physical Chemistry C 
Abstract (english): The adsorption of lysozyme, cytochrome c, and myoglobin, similar-sized globular proteins of approximately 1.5 nm radius, into the mesoporous silica material Santa Barbara Amorphous-15 (SBA-15) with 3.3 nm mean pore radius has been studied photometrically for aqueous solutions containing a single protein type and for binary protein mixtures. Distinct variations in the absolute and relative adsorption behavior are observed as a function of the solution's pH value, and thus pore wall and protein charge. The proteins exhibit the strongest binding below their isoelectric points pI, which indicates the dominance of electrostatic interactions between charged amino acid residues and the - OH groups of the silica surface in the mesopore adsorption process. Moreover, we find for competitive adsorption in the restricted, tubular pore geometry that the protein type which shows the favored binding to the pore wall can entirely suppress the adsorption of the species with lower binding affinity, even though the latter would adsorb quite well from a single component mixture devoid of the strongly binding protein. We suggest that this different physicochemical behavior along with the large specific surface and thus adsorption capability of mesoporous glasses can be exploited for separation of binary mixtures of proteins with distinct pI by adjusting the aqueous solution's pH.
ISSN: 1932-7447
Institute: Werkstoffphysik und -technologie M-22 
Type: (wissenschaftlicher) Artikel
Project: SFB 986, Teilproject B7 - Polymere in grenzflächenbestimmten Geometrien: Struktur, Dynamik und Funktion an planaren und in porösen Hybridsystemen 
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