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HomeNano Hybrids and CompositesNano Hybrids and Composites Vol. 12Folding-Refolding of Ferritin as Template in...

Folding-Refolding of Ferritin as Template in Design of Nanoclusters of Copper and Manganese Oxides

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Abstract:

Bio-templates such as proteins, lipids offer rich structural and functional diversity for the synthesis of nanoparticles by controlling their shape, size and orientation. In this work we have exploited a pH dependent folding-refolding feature of Horse Spleen Apoferritin (HsAFr) to synthesize copper and manganese oxide nanoparticles in a controlled manner. Two methods of preparation were used in this study. In the first method, Copper Sulphate (100 mM) and Manganese Chloride (4.8 mM) have been incubated with the protein and the pH dynamically adjusted for homogeneous incorporation of the metal ions into the HsAFr shell. The second study involved the incorporation of Cu²⁺ and Mn²⁺ inside HsAFr cavity and subsequent designing of nanoclusters of the respective oxides. UV, fluorescence and far-UV circular dichroism (far-UV CD) spectroscopic techniques have been used to study the mineralization effect of the metal inside the HsAFr cavity. Size determination carried out using XRD suggested an average size ranging from 20-30 nm. The EPR of the nanoclusters show that incorporation of Mn²⁺ leads to a characteristic magnetoferritin behavior.

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Nano Hybrids and Composites Vol. 12

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Nano Hybrids and Composites (Volume 12)

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33-41

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https://doi.org/10.4028/www.scientific.net/NHC.12.33

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Online since:

November 2016

Authors:

Harshith Subramanian, Maheshkumar Jaganathan, Aruna Dhathathreyan*

Keywords:

Apoferritin, Copper, Dynamics, Folding, Manganese, Refolding

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© 2017 Trans Tech Publications Ltd. All Rights Reserved

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[1] S. Mornet, S. Vasseur, F. Grasset, E. Duguet, Magnetic nanoparticle design for medical diagnosis and therapy, J. Mat. Chem. 14 (2004) 2161–2175.

DOI: 10.1039/b402025a

[2] F. Sonvico, C. Dubernet, P. Colombo, P. Couvreur, Metallic colloid nanotechnology, applications in diagnosis and therapeutics, Curr. Pharm. Des. 11 (2005) 2091–2105.

DOI: 10.2174/1381612054065738

[3] F.C. Meldrum, V.J. Wade, D.L. Nimmo, B.R. Heywood, S. Mann, Synthesis of inorganic nanophase materials in supramolecular protein cages, Nature 349 (1991) 684-687.

DOI: 10.1038/349684a0

[4] T. Douglas, D.P.E. Dickson, S. Betteridge, J. Charnock, C.D. Garner, S. Mann, Synthesis and Structure of an Iron(III) Sulfide-Ferritin Bioinorganic Nanocomposite, Science 269 (1995) 54-57.

DOI: 10.1126/science.269.5220.54

[5] T. Douglas, M. Young, Host–guest encapsulation of materials by assembled virus protein cages, Nature 393 (1998) 152-155.

DOI: 10.1038/30211

[6] M. Knez, M. Sumser, A.M. Bittner, C. Wege, H. Jeske, T.P. Martin, K. Kern, Spatially selective nucleation of metal clusters on the Tobacco Mosaic Virus, Adv. Funct. Mater. 14 (2004) 116-124.

DOI: 10.1002/adfm.200304376

[7] E. Dujardin, C. Peet, G. Stubbs, J.N. Culver, S. Mann, Organization of metallic nanoparticles using Tobacco Mosaic Virus templates, Nano Lett. 3 (2003) 413-417.

DOI: 10.1021/nl034004o

[8] W. Shenton, S. Mann, H. Colfen, A. Bacher, M. Fischer, Synthesis of nanophase iron oxide in Lumazine Synthase Capsids, Angew. Chem. 113 (2001) 456-459; Angew. Chem. Int. Ed. 40 (2001) 442-445.

DOI: 10.1002/1521-3773(20010119)40:2<442::aid-anie442>3.0.co;2-2

[9] D. Ishii, K. Kinbara, Y. Ishida, N. Ishii, M. Okochi, M. Yohda, T. Aida, Chaperonin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles, Nature 423 (2003) 628-632.

DOI: 10.1038/nature01663

[10] P.M. Harrison, P. Arosio, The ferritins: Molecular properties, iron storage function and cellular regulation, Biochim. Biophys. Acta 1275 (1996) 161-203.

DOI: 10.1016/0005-2728(96)00022-9

[11] M. Ceolín, N. Gálvez, P. Sánchez, B. Fernández, J.M. Domínguez-Vera, Structural aspects of the growth mechanism of Copper nanoparticles inside apoferritin, Eur. J. Inorg. Chem. 2008 (2008) 795–801.

DOI: 10.1002/ejic.200700891

[12] J.D. Klemm, S.L. Schreiber, G.R. Crabtree, Dimerization as a regulatory mechanism in signal transduction, Annu. Rev. Immunol. 16 (1998) 569–592.

DOI: 10.1146/annurev.immunol.16.1.569

[13] A. Fegan, B. White, J.C.T. Carlson, C.R. Wagner, Chemically controlled protein assembly: Techniques and applications, Chem. Rev. 110 (2010) 3315–3336.

DOI: 10.1021/cr8002888

[14] T.W. Corson, N. Aberle, C.M. Crews, Design and applications of bifunctional small molecules: Why two heads are better than one, ACS Chem. Biol. 3 (2008) 677–692.

DOI: 10.1021/cb8001792

[15] F.C. Meldrum, B.R. Heywood, S. Mann, Magnetoferritin: In vitro synthesis of a novel magnetic protein, Science 257 (1992) 522-523.

DOI: 10.1126/science.1636086

[16] G. Liu, H. Wu, J. Wang, Y. Lin, Apoferritin-templated synthesis of metal phosphate nanoparticle labels for electrochemical immunoassay, Small 2 (2006) 1139-1143.

DOI: 10.1002/smll.200600206

[17] T. Douglas, V.T. Stark, Nanophase Cobalt oxyhydroxide mineral synthesized within the protein cage of Ferritin, Inorg. Chem. 39 (2000) 1828-1830.

DOI: 10.1021/ic991269q

[18] J. -W. Kim, S.H. Choi, P.T. Lillehei, S. -H. Chu, G.C. King, G.D. Watt, Cobalt oxide hollow nanoparticles derived by bio-templating, Chem. Commun. (2005) 4101-4103.

DOI: 10.1039/b505097a

[19] R.M. Kramer, C. Li, D.C. Carter, M.O. Stone, R.R. Naik, Engineered protein cages for nanomaterial synthesis, J. Am. Chem. Soc. 126 (2004) 13282-13286.

DOI: 10.1021/ja046735b

[20] T. Ueno, M. Suzuki, T. Goto, T. Matsumoto, K. Nagayama, Y. Watanabe, Size-selective Olefin hydrogenation by a Pd nanocluster provided in an Apoferritin cage, Angew. Chem. 116 (2004) 2581-2584; Angew. Chem. Int. Ed. 43 (2004) 2527-2530.

DOI: 10.1002/anie.200353436

[21] B. Warne, O.I. Kasyutich, E.L. Mayes, J.A.L. Wiggins, K.K.W. Wong, Self assembled nanoparticulate Co: Pt for data storage applications, IEEE Trans. Magn. 36 (2000) 3009-3011.

DOI: 10.1109/20.908658

[22] R. Chiaraluce, V. Consalvi, S. Cavallo, A. Ilari, S. Stefanini, E. Chiancone, The unusual dodecameric ferritin from Listeria innocua dissociates below pH 2. 0, Eur. J. Biochem. 267 (2000) 5733-5741.

DOI: 10.1046/j.1432-1327.2000.01639.x

[23] J. Maheshkumar, B. Sreedhar, B.U. Nair, A. Dhathathreyan, Supported lipid bilayers as templates to design manganese oxide nanoparticles, J. Chem. Sci. 124 (2012) 979-984.

DOI: 10.1007/s12039-012-0295-4

[24] L. Whitemore, B. Wallace, DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data, Nucleic Acids Res. 32 (2004) W668−673.

DOI: 10.1093/nar/gkh371

[25] J.G. Wardeska, B. Viglione, N.D. Chasteen, Metal ion complexes of apoferritin, J. Biol. Chem. 261 (1986) 6677-6683.

DOI: 10.1016/s0021-9258(19)62670-0

[26] C. Jordan, K.M. Bennett, High R1 of Mn2+ adsorbed to hydrophilic pores of magnetoferritin nanoparticles, Proc. Intl. Soc. Mag. Reson. Med. 19 (2011) 321.