Protein-assisted nanoparticle synthesis

Colloids and Surfaces A: Physicochemical and Engineering Aspects

Volumn 282-283, Issue , 2006, Pages 464-470

  Yoshimura, Hideyuki ^a  

^a MEIJI UNIVERSITY   (Japan)

Author keywords

Dps; Ferritin; Indium; Iron; Nanoparticles; Two dimensional array

Indexed keywords

CRYSTALLIZATION; INDIUM; INORGANIC COMPOUNDS; IRON; PROTEINS; SYNTHESIS (CHEMICAL); TWO DIMENSIONAL;

DPS; FERRITIN; NANOPARTICLES (NPS); TWO-DIMENSIONAL ARRAYS;

NANOSTRUCTURED MATERIALS;

DNA BINDING PROTEIN; FERRITIN; INDIUM; IRON; NANOPARTICLE;

AMINO ACID SEQUENCE; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; CRYSTALLIZATION; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; SYNTHESIS;

EID: 33745435178     PISSN: 09277757     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.colsurfa.2006.01.037     Document Type: Article

References (52)

1. Douglas T., and Young M. Host-guest encapsulation of materials by assembled virus protein cages. Nature 393 (1998) 152-155
2. Douglas T., and Stark V.T. Nanophase cobalt oxyhydroxide mineral synthesized within the protein cage of ferritin. Inorg. Chem. 39 (2000) 1828-1830
3. Iwahori K., Yoshizawa K., Muraoka M., and Yamashita I. Fabrication of ZnSe nanoparticles in the apoferritin cavity by designing a slow chemical reaction system. Inorg. Chem. (2005)
4. Kramer R.M., Li C., Carter D.C., Stone M.O., and Naik R.R. Engineered protein cages for nanomaterial synthesis. J. Am. Chem. Soc. 126 (2004) 13282-13286
5. Meldrum F.C., Douglas T., Levi S., Arosio P., and Mann S. Reconstitution of manganese oxide cores in horse spleen and recombinant ferritins. J. Inorg. Biochem. 58 (1995) 59-68
6. Meldrum F.C., Heywood B.R., and Mann S. Magnetoferritin: in vitro synthesis of a novel magnetic protein. Science 257 (1992) 522-523
7. Meldrum F.C., Wade V.J., Nimmo D.L., Heywood B.R., and Mann S. Synthesis of inorganic nanophase materials in supramolecular protein cages. Nature 349 (1991) 684-687
8. Okuda M., Iwahori K., Yamashita I., and Yoshimura H. Fabrication of nickel and chromium nanoparticles using the protein cage of apoferritin. Bitech. Bioeng. 84 (2003) 355-358
9. Okuda M., Kobayashi Y., Suzuki K., Sonoda K., Kondoh T., Wagawa A., Kondo A., and Yoshimura H. Self-organized inorganic nanoparticle arrays on protein lattices. Nano Lett. 5 (2005) 991-993
10. Ueno T., Suzuki M., Goto T., Matsumoto T., Nagayama K., and Watanabe Y. Size-selective olefin hydrogenation by a Pd nanocluster provided in an apoferritin cage. Angew. Chem. Int. Ed. 43 (2004) 2527-2530
11. Warne B., Kasyuich O.I., Mayes E.L., Wiggins J.A.L., and Wong K.K.W. Self assembled nanoparticle Co:Pt for data storage applications. IEEE Trans. Magn. 36 (2000) 3009-3011
12. Wong K.K.W., and Mann S. Biomimetic synthesis of cadmium sulfide-ferritin nanocomposites. Adv. Mater. 8 (1996) 928-932
13. Yamashita I., Hayashi J., and Hara M. Bio-template sysnthesis of uniform CdSe nanoparticles using cage-shaped protein, apoferritin. Chem. Lett. 33 (2004) 1158-1159
14. Harrison P.M., Fischbach F.A., Hoy T.G., and Haggis G.H. Ferric oxyhydroxide core of ferritin. Nature 216 (1967) 1188-1190
15. Allen M., Willits D., Young M., and Douglas T. Constrained synthesis of cobalt oxide nanomaterials in the 12-subunit protein cage from Listeria innocua. Inorg. Chem. 42 (2003) 6300-6305
16. Stefanini S., Cavallo S., Montagnini B., and Chiancone E. Incorporation of iron by the unusual dodecametric ferritin from Listeria innocua. Bichem. J. 338 (1999) 71-75
17. Ilari A., Ceci P., Ferrari D., Rossi G.L., and Chiancone E. Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core. J. Biol. Chem. 277 (2002) 37619-37623
18. Horne R.W. The formation of virus crystalline and paracrystalline arrays for electron microscopy and image analysis. Adv. Virus Res. 24 (1979) 173-221
19. Scheybani T., Yoshimura H., Baumeister W., and Nagayama K. Stabilization of fragile two-dimensional protein crystals at the water-air interface: lattice of apoferritin. Langmuir 12 (1996) 431-435
20. Yoshimura H., Matsumoto M., Endo S., and Nagayama K. Two-dimensional crystallization of protein on mercury. Ultramicroscopy 32 (1990) 265-274
21. Yoshimura H., Scheybani T., Baumeister W., and Nagayama K. Two-dimensional protein array growth in thin layers of protein solution on aqueous subphases. Langmuir 10 (1995) 3290-3295
22. Hainfeld J.F. Uranium-loaded apoferritin with antibodies attached: molecular design for uranium neutron-capture therapy. Proc. Natl. Acad. Sci. USA 89 (1992) 11064-11068
23. Morrissey J.M., Taylor K.D., and Gilman S.D. Ultrasound-mediated release of iron from ferritin. Ultrasound Med. 29 (2003) 1799-1803
24. Kirimura H., Uraoka Y., Fuyuki T., Okuda M., and Yamashita I. Study of low-temperature crystallization of amorphous Si films obtained using ferritin with Ni nanoparticles. Appl. Phys. Lett. 86 (2005) 262106-262108
25. Mayes E., Bewick A., Gleeson D., Hoinville J., Jones R., Kasyuich O., Nartowski A., Warne B., Wiggins J., and Wong K.K.W. Biologically derived nanomagnets in self-organized patterned media. IEEE Trans. Magn. 39 (2003) 624-627
26. Levi S., Santambrogio P., Cozzi A., Rovida E., Corsi B., Tamborini E., Spada S., Albertini A., and Arosio P. The role of the L-chain in ferritin iron incorporation studies of homo and heteropolymers. J. Mol. Biol. 238 (1994) 649-654
27. Banyard S.H., Stammers D.K., and Harrison P.M. Electron density map of apoferritin at 2.8 Å resolution. Nature 271 (1978) 282-284
28. Chasteen N.D., and Harrison P.M. Mineralization in ferritin: an efficient means of iron storage. J. Struct. Biol. 126 (1999) 182-194
29. Yang X., Arosio P., and Chasteen N.D. Molecular diffusion into ferritin: pathways, temperature dependence, incubation time, and concentration effects. Biophys. J. 78 (2000) 2049-2059
30. Jones T., Spencer R., Walsh C., and Mechanism. Kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogues. Biochemistry 17 (1978) 4011-4017
31. Yang D., and Nagayama K. Permeation of small molecules into the cavity of ferritin as revealed by proton nuclear magnetic resonance relaxation. Bichem. J. 307 (1995) 253-256
32. W.H. Massover, Dynamic stability of apoferritin: a new model to explain how impermiable reagents can reduce/capture iron within ferritin, in: R.B. Frankel, R.P. Blakemore (Eds.), Iron Biominerals, Plenum Press, New York, 1990, pp. 349-358.
33. Levi S., Luzzago A., Franceschinelli F., Santambrogio P., Cesareni G., and Arosio P. Mutational analysis of the channel and loop sequences of human ferritin H-chain. Biochem. J. 264 (1989) 381-388
34. Wade V.J., Levi S., Arosio P., Treffry A., Harrison P.M., and Mann S. Influence of site-directed modifications on the formation of iron cores in ferritin. J. Mol. Biol. 221 (1991) 1443-1452
35. Douglas T., and Ripoll D.R. Calculated electrostatic gradients in recombinat human H-chain ferritin. Protein Sci. 7 (1998) 1083-1091
36. Mackle P., Charnock J.M., Garner C.D., Meldrum F.C., and Mann S. Characterization of the manganese core of reconstituted ferritin by X-ray absorption spectroscopy. J. Am. Chem. Soc. 115 (1993) 8471-8472
37. Dedman D.J., Treffry A., and Harrison P.M. Interaction of aluminium citrate with horse spleen ferritin. Biochem. J. 287 (1992) 515-520
38. Fleming J., and Joshi J.G. Ferritin: isolation of aluminium-ferritin complex from brain. Proc. Natl. Acad. Sci. USA 84 (1987) 7866-7870
39. Price D.J., and Joshi J.G. Ferritin: binding of beryllium and other divalent metal ions. J. Biol. Chem. 258 (1983) 10873-10880
40. Price D., and Joshi J.G. Ferritin: a zinc detoxicant and a zinc ion donner. Proc. Natl. Acad. Sci. USA 79 (1982) 3116-3119
41. Clegg G.A., Fitton J.E., Harrison P.M., and Treffry A. Ferritin: molecular structure and iron-storage mechanisms. Prog. Biophys. Molec. Biol. 36 (1980) 56-86
42. Rohrer J.S., Islam Q.T., Watt G.D., Sayers D.E., and Theil E.C. Iron environment in ferritin with large amount of phosphate, from Azotobacter vinelandii and horse spleen, analyzed using extended x-ray absorption fine structure (EXAFS). Biochemistry 29 (1990) 259-264
43. Grant R.A., Filman D.J., Finkel S.E., Kolter R., and Hogle J.M. The crystal structire of Dps, a ferritin homolog that binds and protects DNA. Nature Struct. Biol. 5 (1998) 294-303
44. Ren B., Tibbelin G., Kajino T., Asami O., and Ladenstein R. The multi-layered structure of Dps with a novel di-nuclear ferrocxidase center. J. Mol. Biol. 329 (2003) 467-477
45. Almirón M., Link A.J., Furlong D., and Kolter R. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Gene Dev. 6 (1992) 2646-2654
46. Fromherz P. Electron microscopic studies of lipid protein films. Nature 231 (1971) 267-368
47. Furuno T., Sasabe H., and Ulmer K.L. Binding of ferritin molecules to a charged polypeptide layer of poly-1-benzyl-l-histidine. Thin Solid Films 180 (1989) 23-30
48. Aoyama K., Ogawa K., Kimura Y., and Fujiyoshi Y. A method for 2D crystallization of soluble proteins at liquid-liquid interface. Ultramicroscopy 57 (1995) 345-354
49. Wolf S.G., Frenkiel D., Arad T., Finkel S.E., Kolter R., and Minsky A. DNA protection by stress-induced biocrystallization. Nature 400 (1999) 83-85
50. Yamashita I. Fabrication of a two-dimensional array of nano-particles using ferritin molecule. Thin Solid Films 393 (2001) 12-18
51. Kubota T., Baba T., Samukawa S., Kawashima H., Uraoka Y., Fuyuki T., and Yamashita I. A 7-nm nanocolumn structure fabricated by using a ferritin iron-core mask and low-energy Cl neutral beams. Appl. Phys. Lett. 84 (2003) 1555-1557
52. Jeong G.-H., Yamazaki A., Suzuki S., Yoshimura H., Kobayashi Y., and Homma Y. Cobalt-filled apoferritin for suspended single-walled carbon nanotube growth with narrow diameter distribution. J. Am. Chem. Soc. 127 (2005) 8238-8239