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Identifying specific protein residues that guide surface interactions and orientation on silica nanoparticles.
- Source :
-
Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2013 Aug 27; Vol. 29 (34), pp. 10841-9. Date of Electronic Publication: 2013 Aug 15. - Publication Year :
- 2013
-
Abstract
- We identify specific acylphosphatase (AcP) residues that interact with silica nanoparticles (SNPs) using a combined NMR spectroscopy and proteomics-mass spectrometry approach. AcP associated with 4- and 15-nm diameter SNPs through a common and specific interaction surface formed by amino acids from the two α-helices of the protein. Greater retention of native protein structure was obtained on 4-nm SNPs than on 15-nm particles, presumably due to greater surface curvature-induced protein stabilization with the smaller SNPs. These results demonstrate that proteins may undergo specific and size-dependent orientation on nanoparticle surfaces. Our approach can be broadly applied to various protein-material systems to help understand in much greater detail the protein-nanomaterial interface; it would also encourage better modeling, and thus prediction and design, of the behavior of functional proteins adsorbed onto different surfaces.
Details
- Language :
- English
- ISSN :
- 1520-5827
- Volume :
- 29
- Issue :
- 34
- Database :
- MEDLINE
- Journal :
- Langmuir : the ACS journal of surfaces and colloids
- Publication Type :
- Academic Journal
- Accession number :
- 23906189
- Full Text :
- https://doi.org/10.1021/la401985d