Time-dependent, protein-directed growth of gold nanoparticles within a single crystal of lysozyme
Source abstract
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.
Source: europepmc · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Nanocluster Synthesis and Applications · Gold and Silver Nanoparticles Synthesis and Applications · Nanoparticle-Based Drug Delivery
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (35)
Show source-provided references
1. Daniel, M. C. & Astruc, D. Gold nanoparticles: assembly, supramolecular chemistry, quantum-size-related properties, and applications toward biology, catalysis, and nanotechnology. Chem. Rev. 104, 293–346 (2004).10.1021/cr030698+ ↗
2. Rosi, N. L. & Mirkin, C. A. Nanostructures in biodiagnostics. Chem. Rev. 105, 1547–1562 (2005).10.1021/cr030067f ↗
3. De, M. et al. Sensing of proteins in human serum using conjugates of nanoparticles and green fluorescent protein. Nature Chem. 1, 461–465 (2009).10.1038/nchem.334 ↗
4. Murphy, C. J. et al. Gold nanoparticles in biology: beyond toxicity to cellular imaging. Acc. Chem. Res. 41, 1721–1730 (2008).10.1021/ar800035u ↗
5. Xie, J. P., Zheng, Y. G. & Ying, J. Y. Protein-directed synthesis of highly fluorescent gold nanoclusters. J. Am. Chem. Soc. 131, 888–889 (2009).10.1021/ja806804u ↗
6. Reith, F., Rogers, S. L., McPhail, D. C. & Webb, D. Biomineralization of gold: biofilms on bacterioform gold. Science 313, 233–236 (2006).10.1126/science.1125878 ↗
7. Reith, F. et al. Mechanisms of gold biomineralization in the bacterium Cupriavidus metallidurans. Proc. Natl Acad. Sci. USA 106, 17757–17762 (2009).10.1073/pnas.0904583106 ↗
8. Lengke, M. F. & Southam, G. The effect of thiosulfate-oxidizing bacteria on the stability of the gold–thiosulfate complex. Geochim. Cosmochim. Acta 69, 3759–3772 (2005).10.1016/j.gca.2005.03.012 ↗
9. Karthikeyan, S. & Beveridge, T. J. Pseudomonas aeruginosa biofilms react with and precipitate toxic soluble gold. Environ. Microbiol. 4, 667–675 (2002).10.1046/j.1462-2920.2002.00353.x ↗
10. Kashefi, K., Tor, J. M., Nevin, K. P. & Lovley, D. R. Reductive precipitation of gold by dissimilatory Fe(III)-reducing bacteria and archaea. Appl. Environ. Microbiol. 67, 3275–3279 (2001).10.1128/AEM.67.7.3275-3279.2001 ↗
11. Karamushka, V. I., Ulberg, Z. R. & Gruzina, T. G. The role of membrane processes in bacterial accumulation of Au(III) and Au(0). Ukr. Biokhimicheskii Zhurnal 62, 76–82 (1990).
12. Carney, C. K., Harry, S. R., Sewell, S. L. & Wright, D. W. Detoxification biominerals. Top. Curr. Chem. 270, 155–185 (2007).10.1007/128_050 ↗
13. Mann, S. (eds) Biomineralization: Principles and Concepts in Bioinorganic Materials Chemistry (Oxford Univ. Press, 2001).10.1093/oso/9780198508823.001.0001 ↗
14. Meldrum, F. C., Wade, V. J., Nimmo, D. L., Heywood, B. R. & Mann, S. Synthesis of inorganic nanophase materials in supramolecular protein cages. Nature 349, 684–687 (1991).10.1038/349684a0 ↗
15. Uchida, M. et al. Biological containers: protein cages as multifunctional nanoplatforms. Adv. Mater. 19, 1025–1042 (2007).10.1002/adma.200601168 ↗
16. Medalsy, I. et al. SP1 protein-based nanostructures and arrays. Nano Lett. 8, 473–477 (2008).10.1021/nl072455t ↗
17. Butts, C. A. et al. Directing noble metal ion chemistry within a designed ferritin protein. Biochemistry 47, 12729–12739 (2008).10.1021/bi8016735 ↗
18. Ueno, T. et al. Process of accumulation of metal ions on the interior surface of apo-ferritin: crystal structures of a series of apo-ferritins containing variable quantities of Pd(II) Ions. J. Am. Chem. Soc. 131, 5094–5100 (2009).10.1021/ja806688s ↗
19. Ueno, T., Abe, S., Yokoi, N. & Watanabe, Y. Coordination design of artificial metalloproteins utilizing protein vacant space. Coord. Chem. Rev. 251, 2717–2731 (2007).10.1016/j.ccr.2007.04.007 ↗
20. Dickerson, M. B., Sandhage, K. H. & Naik, R. R. Protein- and peptide-directed syntheses of inorganic materials. Chem. Rev. 108, 4935–4978 (2008).10.1021/cr8002328 ↗
21. Margolin, A. L. & Navia, M. A. Protein crystals as novel catalytic materials. Angew. Chem. Int. Ed. 40, 2205–2222 (2001).10.1002/1521-3773(20010618)40:12<2204::AID-ANIE2204>3.0.CO;2-J ↗
22. Koshiyama, T. et al. Modification of porous protein crystals in development of biohybrid materials. Bioconjugate Chem. 21, 264–269 (2010).10.1021/bc9003052 ↗
23. Falkner, J. C. et al. Virus crystals as nanocomposite scaffolds. J. Am. Chem. Soc. 127, 5274–5275 (2005).10.1021/ja044496m ↗
24. Guli, M., Lambert, E. M., Li, M. & Mann, S. Template-directed synthesis of nanoplasmonic arrays by intracrystalline metalization of cross-linked lysozyme crystals. Angew. Chem. Int. Ed. 49, 520–523 (2010).10.1002/anie.200905070 ↗
25. Jolles, P. & Jolles, J. Whats new in lysozyme research—always a model system, today as yesterday. Mol. Cell. Biochem. 63, 165–189 (1984).10.1007/BF00285225 ↗
26. Sanders, L. K. et al. Control of electrostatic interactions between F-actin and genetically modified lysozyme in aqueous media. Proc. Natl Acad. Sci. USA 104, 15994–15999 (2007).10.1073/pnas.0705898104 ↗
27. Kawamichi, T., Haneda, T., Kawano, M. & Fujita, M. X-ray observation of a transient hemiaminal trapped in a porous network. Nature 461, 633–635 (2009).10.1038/nature08326 ↗
28. Li, H. Y., Xin, H. L., Muller, D. A. & Estroff, L. A. Visualizing the 3D internal structure of calcite single crystals grown in agarose hydrogels. Science 326, 1244–1247 (2009).10.1126/science.1178583 ↗
29. Hodzhaoglu, F., Kurniawan, F., Mirsky, V. & Nanev, C. Gold nanoparticles induce protein crystallization. Cryst. Res. Technol. 43, 588–593 (2008).10.1002/crat.200811125 ↗
30. Arslan, I., Yates, T. J. V., Browning, N. D. & Midgley, P. A. Embedded nanostructures revealed in three dimensions. Science 309, 2195–2198 (2005).10.1126/science.1116745 ↗
31. Browning, N. D., Chisholm, M. F. & Pennycook, S. J. Atomic-resolution chemical analysis using a scanning transmission electron microscope. Nature 366, 143–146 (1993).10.1038/366143a0 ↗
32. Puddephatt, R. J. (eds) The Chemistry of Gold (Topics in Inorganic and General Chemistry, Monograph 16) (Elsevier Scientific Publishing, 1978).
33. Pyykko, P. Theoretical chemistry of gold. Angew. Chem. Int. Ed. 43, 4412–4456 (2004).10.1002/anie.200300624 ↗
34. Ralle, M., Lutsenko, S. & Blackburn, N. J. X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines. J. Biol. Chem. 278, 23163–23170 (2003).10.1074/jbc.M303474200 ↗
35. Lichtenegger, H. C., Schoberl, T., Bartl, M. H., Waite, H. & Stucky, G. D. High abrasion resistance with sparse mineralization: copper biomineral in worm jaws. Science 298, 389–392 (2002).10.1126/science.1075433 ↗