Probing protein adsorption onto mercaptoundecanoic acid stabilized gold nanoparticles and surfaces by quartz crystal microbalance and zeta-potential measurements

The adsorption characteristics of three proteins [bovine serum albumin (BSA), myoglobin (Mb), and cytochrome c (CytC)] onto self-assembled monolayers of mercaptoundecanoic acid (MUA) on both gold nanoparticles (AuNP) and gold surfaces (Au) are described. The combination of quartz crystal microbalanc...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 23(2007), 11 vom: 22. Mai, Seite 6053-62
1. Verfasser: Kaufman, Eric D (VerfasserIn)
Weitere Verfasser: Belyea, Jennifer, Johnson, Marcus C, Nicholson, Zach M, Ricks, Jennifer L, Shah, Pavak K, Bayless, Michael, Pettersson, Torbjörn, Feldotö, Zsombor, Blomberg, Eva, Claesson, Per, Franzen, Stefan
Format: Aufsatz
Sprache:English
Veröffentlicht: 2007
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Coated Materials, Biocompatible Fatty Acids Myoglobin Proteins undecanoic acid 138ON3IIQG Quartz mehr... 14808-60-7 Serum Albumin, Bovine 27432CM55Q Gold 7440-57-5 Cytochromes c 9007-43-6
Beschreibung
Zusammenfassung:The adsorption characteristics of three proteins [bovine serum albumin (BSA), myoglobin (Mb), and cytochrome c (CytC)] onto self-assembled monolayers of mercaptoundecanoic acid (MUA) on both gold nanoparticles (AuNP) and gold surfaces (Au) are described. The combination of quartz crystal microbalance measurements with dissipation (QCM-D) and pH titrations of the zeta-potential provide information on layer structure, surface coverage, and potential. All three proteins formed adsorption layers consisting of an irreversibly adsorbed fraction and a reversibly adsorbed fraction. BSA showed the highest affinity for the MUA/Au, forming an irreversibly adsorbed rigid monolayer with a side-down orientation and packing close to that expected in the jamming limit. In addition, BSA showed a large change in the adsorbed mass due to reversibly bound protein. The data indicate that the irreversibly adsorbed fraction of CytC is a monolayer structure, whereas the irreversibly adsorbed Mb is present in form of a bilayer. The observation of stable BSA complexes on MUA/AuNPs at the isoelectric point by zeta-potential measurements demonstrates that BSA can sterically stabilize MUA/AuNP. On the other hand, MUA/AuNP coated with either Mb or CytC formed a reversible flocculated state at the isoelectric point. The colloidal stability differences may be correlated with weaker binding in the reversibly bound overlayer in the case of Mb and CytC as compared to BSA
Beschreibung:Date Completed 11.07.2007
Date Revised 16.11.2017
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827