Issue 10, 2018

Structure and formation of highly luminescent protein-stabilized gold clusters

Abstract

Highly luminescent gold clusters simultaneously synthesized and stabilized by protein molecules represent a remarkable category of nanoscale materials with promising applications in bionanotechnology as sensors. Nevertheless, the atomic structure and luminescence mechanism of these gold clusters are still unknown after several years of developments. Herein, we report findings on the structure, luminescence and biomolecular self-assembly of gold clusters stabilized by the large globular protein, bovine serum albumin. We highlight the surprising identification of interlocked gold-thiolate rings as the main gold structural unit. Importantly, such gold clusters are in a rigidified state within the protein scaffold, offering an explanation for their highly luminescent character. Combined free-standing cluster synthesis (without protecting protein scaffold) with rigidifying and un-rigidifying experiments, were designed to further verify the luminescence mechanism and gold atomic structure within the protein. Finally, the biomolecular self-assembly process of the protein-stabilized gold clusters was elucidated by time-dependent X-ray absorption spectroscopy measurements and density functional theory calculations.

Graphical abstract: Structure and formation of highly luminescent protein-stabilized gold clusters

Supplementary files

Article information

Article type
Edge Article
Submitted
28 Nov. 2017
Accepted
05 Febr. 2018
First published
05 Febr. 2018
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2018,9, 2782-2790

Structure and formation of highly luminescent protein-stabilized gold clusters

D. M. Chevrier, V. D. Thanthirige, Z. Luo, S. Driscoll, P. Cho, M. A. MacDonald, Q. Yao, R. Guda, J. Xie, E. R. Johnson, A. Chatt, N. Zheng and P. Zhang, Chem. Sci., 2018, 9, 2782 DOI: 10.1039/C7SC05086K

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