Journal
JOURNAL OF NANOPARTICLE RESEARCH
Volume 13, Issue 2, Pages 625-636Publisher
SPRINGER
DOI: 10.1007/s11051-010-0057-5
Keywords
Gold nanoparticles; Chemical modification; Nanoparticle-protein interactions; Aggregation; Protein modification; Nanobiotechnology
Categories
Funding
- Robert A. Welch Foundation [C-576]
- National Science Foundation Center for Biological and Environmental Nanotechnology, NSF-NSEC [EEC-0647452]
- W.M. Keck Center for Interdisciplinary Bioscience Training of the Gulf Coast Consortia (NIH) [1 T90 DK70121-01, 1 R90 DK71504-01]
- Kobayashi Fellowship
- Methodist Hospital Research Institute
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Gold nanoparticles (AuNP) can interact with a wide range of molecules including proteins. Whereas significant attention has focused on modifying the nanoparticle surface to regulate protein-AuNP assembly or influence the formation of the protein corona, modification of the protein surface as a mechanism to modulate protein-AuNP interaction has been less explored. Here, we examine this possibility utilizing three small globular proteins-lysozyme with high isoelectric point (pI) and established interactions with AuNP; alpha-lactalbumin with similar tertiary fold to lysozyme but low pI; and myoglobin with a different globular fold and an intermediate pI. We first chemically modified these proteins to alter their charged surface functionalities, and thereby shift protein pI, and then applied multiple methods to assess protein-AuNP assembly. At pH values lower than the anticipated pI of the modified protein, AuNP exposure elicits changes in the optical absorbance of the protein-NP solutions and other properties due to aggregate formation. Above the expected pI, however, protein-AuNP interaction is minimal, and both components remain isolated, presumably because both species are negatively charged. These data demonstrate that protein modification provides a powerful tool for modulating whether nanoparticle-protein interactions result in material aggregation. The results also underscore that naturally occurring protein modifications found in vivo may be critical in defining nanoparticle-protein corona compositions.
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