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  Decoding biomineralization : interaction of a Mad10 derived-peptide with magnetite thin films

Pohl, A., Berger, F., Sullan, R. M., Valverde-Tercedor, C., Freindl, K., Spiridis, N., et al. (2019). Decoding biomineralization: interaction of a Mad10 derived-peptide with magnetite thin films. Nano Letters, 19(11), 8207-8215. doi:10.1021/acs.nanolett.9b03560.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0004-C7E4-A Version Permalink: http://hdl.handle.net/21.11116/0000-0007-71A4-0
Genre: Journal Article

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 Creators:
Pohl, Anna1, 2, Author              
Berger, Florian, Author
Sullan, Ruby M.2, Author              
Valverde-Tercedor, Carmen1, Author              
Freindl, Kinga, Author
Spiridis, Nika, Author
Lefevre, Christopher, Author
Menguy, Nicolas, Author
Klumpp, Stefan3, Author              
Blank, Kerstin G.2, Author              
Faivre, Damien1, Author              
Affiliations:
1Damien Faivre, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863290              
2Kerstin Blank, Mechano(bio)chemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2301698              
3Stefan Klumpp, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863329              

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Free keywords: magnetite, magnetotactic bacteria, magnetite-binding peptide, single molecule force spectroscopy, biomineralization, organics-inorganics interaction
 Abstract: Protein-surface interactions play a pivotal role in processes as diverse as biomineralization, biofouling and the cellular response to medical implants. In biomineralization processes, biomacromolecules control mineral deposition and architecture via complex and often unknown mechanisms. For studying these mechanisms, the formation of magnetite nanoparticles in magnetotactic bacteria has become an excellent model system. Most interestingly, nanoparticle morphologies have been discovered that defy crystallographic rules, e.g. in the species Desulfamplus magnetovallimortis strain BW-1. In certain conditions, this strain mineralizes bullet-shaped magnetite nanoparticles, which exhibit defined (111) crystal faces and are elongated along the [100] direction. We hypothesize that surface-specific protein interactions break the nanoparticle symmetry, inhibiting the growth of certain crystal faces thereby favoring the growth of others. Screening the genome of BW-1, we identified Mad10 (Magnetosome-associated deep-branching) as a potential magnetite-binding protein. Using atomic force microscope (AFM)-based single-molecule force spectroscopy, we show that a Mad10-derived peptide, which represents the most conserved region of Mad10, binds strongly to (100)- and (111)-oriented single-crystalline magnetite thin films. The peptide-magnetite interaction is thus material but not crystal face-specific. It is characterized by broad rupture force distributions that do not depend on the retract speed of the AFM cantilever. To account for these experimental findings, we introduce a three-state model that incorporates fast rebinding. The model suggests that the peptide-surface interaction is strong in the absence of load, which is a direct result of this fast rebinding process. Overall, our study sheds light on the kinetic nature of peptide-surface interactions and introduces a new magnetite-binding peptide with potential use as a functional coating for magnetite nanoparticles in biotechnological and biomedical applications.

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 Dates: 2019-09-302019
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: DOI: 10.1021/acs.nanolett.9b03560
Other: OA?
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Title: Nano Letters
  Abbreviation : Nano Lett.
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 19 (11) Sequence Number: - Start / End Page: 8207 - 8215 Identifier: ISSN: 1530-6984