Journal
RSC ADVANCES
Volume 2, Issue 31, Pages 11704-11711Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2ra21931j
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Funding
- Department of Chemical Engineering, NTNU
- Research Council of Norway (NFR) within the FRINAT [177556/V30]
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Small noble metal nanoclusters can be formed in situ by direct reduction and stabilization of a metal precursor by biomolecules such as proteins. Considering the diversity in amino acid composition of proteins, and hence their reductive ability, a general method for synthesis of gold nanoclusters using proteins is presented here. A range of proteins (bovine serum albumin, fibrinogen, alpha-lactalbumin, lysozyme, cytochrome c, myoglobin, beta-lactoglobulin and alpha-chymotrypsin) have been studied, based on size, isoelectric point, flexibility and 3-dimensional structure. Results show protein-gold nanoconstructs with complex protein-specific photophysical properties. The effect on the 3-dimensional conformation of the proteins upon formation of gold nanoclusters and/or nanoparticles within the protein structure is also shown to be highly protein-dependent. A general mechanism for the formation of protein-gold nanoconstructs is proposed, based on charge density matching, yielding a high local concentration of the metal precursor on the protein structure which in turn can nucleate, grow and be stabilized by amino acid residues in the protein.
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