Structure and formation of highly luminescent protein-stabilized gold clusters. Issue 10 (14th February 2018)

• Record Type: Journal Article
• Authors: Chevrier, D. M.; Thanthirige, V. D.; Luo, Z.; Driscoll, S.; Cho, P.; MacDonald, M. A.; Yao, Q.; Guda, R.; Xie, J.; Johnson, E. R.; Chatt, A.; Zheng, N.; Zhang, P.
• Is Part Of: Chemical science. Volume 9:Issue 10(2018)
• Page Start: 2782
• Page End: 2790
• Publication Date: 2018-02-14
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c7sc05086k
• Languages: English
• ISSNs: 2041-6520

Abstract

Abstract : Findings on the structure and formation of luminescent protein-stabilized gold clusters reveal interlocked gold-thiolate rings and a unique bio-assembled pathway. 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.