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Cited by 172

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Probing Protein Adsorption onto Mercaptoundecanoic Acid Stabilized Gold Nanoparticles and Surfaces by Quartz Crystal Microbalance and ζ-Potential Measurements

Kaufman, Eric D., 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·2007·Langmuir

Abstract

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.

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Crossref · 10.1021/la063725a

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Metadata

Authors
Kaufman, E. D., Belyea, J., Johnson, M. C., Nicholson, Z. M., Ricks, J. L., Shah, P. K., Bayless, M., Pettersson, T., Feldotö, Z., Blomberg, E., Claesson, P., & Franzen, S.
Venue
Langmuir
Published
2007-04-28
Volume
23
Issue
11
Pages
6053-6062
ISSN
  • 0743-7463 (ISSN-L)
  • 1520-5827
OpenAlex
W2023119820
Cited by
172
References
1
FWCI
6.59
Type
journal article
Language
en
Open access
closed

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