Journal
SMALL
Volume 13, Issue 18, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/smll.201603748
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Funding
- Army Research Office [W911NF-11-1-0251]
- National Science Foundation [CHE 1506273]
- NIH (National Institutes of Health) Ruth L. Kirschstein National Research Service [GM108298]
- Direct For Mathematical & Physical Scien [1506273] Funding Source: National Science Foundation
- Division Of Chemistry [1506273] Funding Source: National Science Foundation
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Understanding the fundamental biophysics behind protein-nanoparticle (NP) interactions is essential for the design and engineering bio-NP systems. The authors describe the development of a coarse-grained protein-NP model that utilizes a structure centric protein model. A key feature of the protein-NP model is the quantitative inclusion of the hydrophobic character of residues in the protein and their interactions with the NP surface. In addition, the curvature of the NP is taken into account, capturing the protein behavior on NPs of different size. The authors evaluate this model by comparison with experimental results for structure and adsorption of a model protein interacting with an NP. It is demonstrated that the simulation results recapitulate the structure of the small alpha/beta protein GB1 on the NP for data from circular dichroism and fluorescence spectroscopy. In addition, the calculated protein adsorption free energy agrees well with the experimental value. The authors predict the dependence of protein folding on the NP size, surface chemistry, and temperature. The model has the potential to guide NP design efforts by predicting protein behavior on NP surfaces with various chemical properties and curvatures.
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