Hostname: page-component-78c5997874-mlc7c Total loading time: 0 Render date: 2024-11-17T06:04:18.607Z Has data issue: false hasContentIssue false
  • English
  • Français

Understanding Magnetite Biomineralisation: The Effect of Short Amino Acid Sequences on the {100} and the {111} Surface

Published online by Cambridge University Press:  12 March 2013

Amy E. Monnington  and
David J. Cooke
Amy E. Monnington
Affiliation:
Department of Chemical & Biological Sciences, University of Huddersfield, Queensgate, Huddersfield, HD1 3DH, UK
David J. Cooke
Affiliation:
Department of Chemical & Biological Sciences, University of Huddersfield, Queensgate, Huddersfield, HD1 3DH, UK
Get access

Abstract

Magnetite (Fe3O4) formation within Magnetospirillum magneticum strain AMB-1 occurs under the influence of the Mms6 protein. It is hypothesised that if key iron binding sites within the C-terminus of the Mms6 protein are substituted for alanine, the protein’s overall iron binding ability is diminished. In this study, an atomistic model of Mms6-driven magnetite formation was developed and the attachment of series amino acid repeats (alanine-alanine, alanine-glutamic acid & glutamic acid-glutamic acid) to the {100} & {111} magnetite surfaces were investigated. Our results suggest the substitution of glutamic acid for alanine residues significantly reduces iron binding affinity of the system, thus confirming the hypothesis. In addition, it is shown that the surface of preferable attachment is the {111} magnetite surface.

Keywords

biomaterialcrystal growthFe
Type
Articles
Information
MRS Online Proceedings Library (OPL) , Volume 1498: Symposium R – Biomimetic, Bio-inspired and Self-Assembled Materials for Engineered Surfaces and Applications , 2013 , pp. 239 - 245
Copyright
Copyright © Materials Research Society 2013 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Schopf, J.W., Barghoorn, E.S., Morton, D.M., Gordon, R.O., Science, 149, 1365 (1965).CrossRefGoogle Scholar
Blakemore, R., Science, 190, 377 (1975).CrossRefGoogle Scholar
Bazylinski, D.A., Frankel, R.B., Nature Reviews Microbiology, 2, 217 (2004).CrossRefGoogle Scholar
Gorby, Y.A., Beveridge, T.J., Blakemore, R.P., Journal of Bacteriology, 170, 834 (1988).CrossRefGoogle Scholar
Meldrum, F.C., Mann, S., Heywood, B.R., Frankel, R.B., Bazylinski, D.A., Proceedings of the Royal Society of London. Series B: Biological Sciences, 251, 231 (1993); 251, 237(1993).Google Scholar
Arakaki, A., Masuda, F., Amemiya, Y., Tanaka, T., Matsunaga, T., Journal of colloid and interface science, 343, 65 (2010).CrossRefGoogle Scholar
Matsunaga, T., Okamura, Y., Trends in Microbiology, 11, 536 (2003).CrossRefGoogle Scholar
Bahaj, A.S., Croudace, I.W., James, P.A.B., Moeschler, F.D., Warwick, P.E., Journal of magnetism and magnetic materials, 184, 241 (1998).CrossRefGoogle Scholar
Bulte, J.W.M, Douglas, T., Mann, S., Frankel, R.B., Moskowitz, B.M., Brooks, R.A., Baumgarner, C.D., Vymazal, J., Strub, M.P, Frank, J.A., Investigative radiology, 29, S214 (1994); Journal of Magnetic Resonance Imaging, 4, 497(1994).CrossRefGoogle Scholar
Sun, C., Lee, J.S.H., Zhang, M., Advanced drug delivery reviews, 60, 1252 (2008).CrossRefGoogle Scholar
Nakamura, N., Burgess, J.G., Yagiuda, K., Kudo, S., Sakaguchi, T., Matsunaga, T., Analytical Chemistry, 65, 2036 (1993).CrossRefGoogle Scholar
Nakamura, N., Matsunaga, T., Analytica Chimica Acta, 281, 585 (1993).CrossRefGoogle Scholar
Hergt, R., Hiergeist, R., Zeisberger, M., Schüler, D., Heyen, U., Hilger, I., Kaiser, W.A., Journal of Magnetism and Magnetic Materials, 293, 80 (2005); R. Hergt, S. Dutz, ibid., 311, 187 (2007).CrossRefGoogle Scholar
Dobson, J., Drug Development Research, 67, 55 (2006); Gene Therapy, 13, 283 (2006).CrossRefGoogle Scholar
Lübbe, A.S., Alexiou, C., Bergemann, C., Journal of Surgical Research, 95, 200 (2001).CrossRefGoogle Scholar
Smith, W., Forester, T.R., DL_POLY is a package of molecular simulation routines, copyright The Council for the Central Laboratory of the Research Councils, Daresbury Laboratory at Daresbury, Nr. Warrington, (1996); Journal of Molecular Graphics, 14, 136(1996).Google Scholar
Verlet, L., Phys. Rev., 159, 98 (1967).CrossRefGoogle Scholar
Ewald, P.P., Annalen der Physik, 64, 253 (1921).CrossRefGoogle Scholar
Cornell, W.D., Cieplak, P., Bayly, C.I., Gould, I.R., Merz, K.M., Ferguson, D.M., Spellmeyer, D.C., Fox, T., Caldwell, J.W., Kollman, P.A., Journal of the American Chemical Society, 117, 5179 (1995).CrossRefGoogle Scholar
Kerisit, S., Geochimica et Cosmochimica Acta, 75, 2043 (2011).CrossRefGoogle Scholar
Schmitt, U.W., Voth, G.A., J. Chem. Phys., 111, 9361 (2000)CrossRefGoogle Scholar
Watson, G.W., Kelsey, E.T., de Leeuw, N.H., Harris, D.J., Parker, S.C., J. Chem. Soc., Faraday Trans., 92, 433 (1996).Google Scholar
Hill, T.L., Statistical Mechanics, (McGraw-Hill, New York, 1956).Google Scholar
Staniland, S., Rawlings, A., Bramble, J., (private communication)Google Scholar