Size Evolution of Protein-Protected Gold Clusters in Solution: A Combined SAXS-MS Investigation

Title
Size Evolution of Protein-Protected Gold Clusters in Solution: A Combined SAXS-MS Investigation
Authors
이해원
Issue Date
2015-01
Publisher
AMER CHEMICAL SOC
Citation
JOURNAL OF PHYSICAL CHEMISTRY C, v. 119, NO 4, Page. 2148-2157
Abstract
We report a combined small-angle X-ray scattering (SAXS) and mass spectrometric (MS) study of the growth of gold clusters within proteins, in the solution state. Two different proteins, namely, lysozyme (Lyz) and bovine serum albumin (BSA), were used for this study. SAXS study of clusters grown in Lyz shows the presence of a 0.8 nm gold core, which is in agreement with the Au-10 cluster observed in MS. Dynamic light scattering suggests the size of the cluster core to be 1.2 nm. For BSA, however, a bigger core size was observed, comparable to the Au-33 core obtained in MS. Concentration- and time-dependent data do not show much change in the core size in both SAXS and MS investigations. When metal-protein adducts were incubated for longer time in solution, nanoparticles were formed and protein size decreased, possibly due to the fragmentation of the latter during nanoparticle formation. The data are in agreement with dynamic light scattering studies. This work helps to directly visualize cluster growth within protein templates in solution.
URI
http://hdl.handle.net/20.500.11754/21281http://pubs.acs.org/doi/abs/10.1021/jp509332j
ISSN
1932-7447
DOI
http://dx.doi.org/10.1021/jp509332j
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COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > CHEMISTRY(화학과) > Articles
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