3P66

Time-dependent and Protein-directed In Situ Growth of Gold Nanoparticles in a Single Crystal of Lysozyme

Summary for 3P66

• Entry DOI: 10.2210/pdb3p66/pdb
• Related: 3P4Z 3P64 3P65 3P68
• Descriptor: Lysozyme C, GOLD 3+ ION (3 entities in total)
• Functional Keywords: hydrolase, binding sites, bio-nano hybrids, old nanoparticles, porous materials
• Biological source: Gallus gallus (bantam,chickens)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 15906.90

Authors

Wei, H.,Wang, Z.,Zhang, J.,House, S.,Gao, Y.-G.,Yang, L.,Robinson, H.,Tan, L.H.,Xing, H.,Hou, C.,Robertson, I.M.,Zuo, J.-M.,Lu, Y. (deposition date: 2010-10-11, release date: 2011-02-09, Last modification date: 2024-10-16)

Primary citation

Wei, H.,Wang, Z.,Zhang, J.,House, S.,Gao, Y.G.,Yang, L.,Robinson, H.,Tan, L.H.,Xing, H.,Hou, C.,Robertson, I.M.,Zuo, J.M.,Lu, Y.
Time-dependent, protein-directed growth of gold nanoparticles within a single crystal of lysozyme.
Nat Nanotechnol, 6:93-97, 2011

PubMed Abstract: Gold nanoparticles are useful in biomedical applications due to their distinct optical properties and high chemical stability. Reports of the biogenic formation of gold colloids from gold complexes has also led to an increased level of interest in the biomineralization of gold. However, the mechanism responsible for biomolecule-directed gold nanoparticle formation remains unclear due to the lack of structural information about biological systems and the fast kinetics of biomimetic chemical systems in solution. Here we show that intact single crystals of lysozyme can be used to study the time-dependent, protein-directed growth of gold nanoparticles. The protein crystals slow down the growth of the gold nanoparticles, allowing detailed kinetic studies to be carried out, and permit a three-dimensional structural characterization that would be difficult to achieve in solution. Furthermore, we show that additional chemical species can be used to fine-tune the growth rate of the gold nanoparticles.

PubMed: 21278750
DOI: 10.1038/nnano.2010.280

Experimental method

X-RAY DIFFRACTION (1.36 Å)