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Issue 5, 2013
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Protein-encapsulated gold cluster aggregates: the case of lysozyme

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Abstract

We report the evolution and confinement of atomically precise and luminescent gold clusters in a small protein, lysozyme (Lyz) using detailed mass spectrometric (MS) and other spectroscopic investigations. A maximum of 12 Au0 species could be bound to a single Lyz molecule irrespective of the molar ratio of Lyz : Au3+ used for cluster growth. The cluster-encapsulated protein also forms aggregates similar to the parent protein. Time dependent studies reveal the emergence of free protein and the redistribution of detached Au atoms, at specific Lyz to Au3+ molar ratios, as a function of incubation time, proposing inter-protein metal ion transfer. The results are in agreement with the studies of inter-protein metal transfer during cluster growth in similar systems. We believe that this study provides new insights into the growth of clusters in smaller proteins.

Graphical abstract: Protein-encapsulated gold cluster aggregates: the case of lysozyme

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Supplementary files

Article information


Submitted
15 Oct 2012
Accepted
26 Dec 2012
First published
04 Jan 2013

Nanoscale, 2013,5, 2009-2016
Article type
Paper

Protein-encapsulated gold cluster aggregates: the case of lysozyme

A. Baksi, P. L. Xavier, K. Chaudhari, N. Goswami, S. K. Pal and T. Pradeep, Nanoscale, 2013, 5, 2009
DOI: 10.1039/C2NR33180B

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