Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis

Andrea E. Rawlings, Jonathan P. Bramble, Anna A. S. Tang, Lori A. Somner, Amy E. Monnington, David J. Cooke, Michael J. Mcpherson, Darren C. Tomlinson, Sarah S. Staniland

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Adhirons are robust, well expressing, peptide display scaffold proteins, developed as an effective alternative to traditional antibody binding proteins for highly specific molecular recognition applications. This paper reports for the first time the use of these versatile proteins for material binding, and as tools for controlling material synthesis on the nanoscale. A phage library of Adhirons, each displaying two variable binding loops, was screened to identify specific proteins able to interact with [100] faces of cubic magnetite nanoparticles. The selected variable regions display a strong preference for basic residues such as lysine. Molecular dynamics simulations of amino acid adsorption onto a [100] magnetite surface provides a rationale for these interactions, with the lowest adsorption energy observed with lysine. These proteins direct the shape of the forming nanoparticles towards a cubic morphology in room temperature magnetite precipitation reactions, in stark contrast to the high temperature, harsh reaction conditions currently used to produce cubic nanoparticles. These effects demonstrate the utility of the selected Adhirons as novel magnetite mineralization control agents using ambient aqueous conditions. The approach we outline with artificial protein scaffolds has the potential to develop into a toolkit of novel additives for wider nanomaterial fabrication.
LanguageEnglish
Pages5586-5594
Number of pages9
JournalChemical Science
Volume6
Issue number10
DOIs
Publication statusPublished - 30 Jun 2015

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Ferrosoferric Oxide
Bacteriophages
Display devices
Nanoparticles
Proteins
Scaffolds
Lysine
Magnetite Nanoparticles
Adsorption
Molecular recognition
Nanostructured materials
Molecular dynamics
Carrier Proteins
Amino Acids
Fabrication
Temperature
Peptides
Antibodies
Computer simulation

Cite this

Rawlings, A. E., Bramble, J. P., Tang, A. A. S., Somner, L. A., Monnington, A. E., Cooke, D. J., ... Staniland, S. S. (2015). Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis. Chemical Science, 6(10), 5586-5594. https://doi.org/10.1039/C5SC01472G
Rawlings, Andrea E. ; Bramble, Jonathan P. ; Tang, Anna A. S. ; Somner, Lori A. ; Monnington, Amy E. ; Cooke, David J. ; Mcpherson, Michael J. ; Tomlinson, Darren C. ; Staniland, Sarah S. / Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis. In: Chemical Science. 2015 ; Vol. 6, No. 10. pp. 5586-5594.
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Rawlings, AE, Bramble, JP, Tang, AAS, Somner, LA, Monnington, AE, Cooke, DJ, Mcpherson, MJ, Tomlinson, DC & Staniland, SS 2015, 'Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis', Chemical Science, vol. 6, no. 10, pp. 5586-5594. https://doi.org/10.1039/C5SC01472G

Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis. / Rawlings, Andrea E.; Bramble, Jonathan P.; Tang, Anna A. S.; Somner, Lori A.; Monnington, Amy E.; Cooke, David J.; Mcpherson, Michael J.; Tomlinson, Darren C.; Staniland, Sarah S.

In: Chemical Science, Vol. 6, No. 10, 30.06.2015, p. 5586-5594.

Research output: Contribution to journalArticle

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T1 - Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis

AU - Rawlings, Andrea E.

AU - Bramble, Jonathan P.

AU - Tang, Anna A. S.

AU - Somner, Lori A.

AU - Monnington, Amy E.

AU - Cooke, David J.

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AU - Tomlinson, Darren C.

AU - Staniland, Sarah S.

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AB - Adhirons are robust, well expressing, peptide display scaffold proteins, developed as an effective alternative to traditional antibody binding proteins for highly specific molecular recognition applications. This paper reports for the first time the use of these versatile proteins for material binding, and as tools for controlling material synthesis on the nanoscale. A phage library of Adhirons, each displaying two variable binding loops, was screened to identify specific proteins able to interact with [100] faces of cubic magnetite nanoparticles. The selected variable regions display a strong preference for basic residues such as lysine. Molecular dynamics simulations of amino acid adsorption onto a [100] magnetite surface provides a rationale for these interactions, with the lowest adsorption energy observed with lysine. These proteins direct the shape of the forming nanoparticles towards a cubic morphology in room temperature magnetite precipitation reactions, in stark contrast to the high temperature, harsh reaction conditions currently used to produce cubic nanoparticles. These effects demonstrate the utility of the selected Adhirons as novel magnetite mineralization control agents using ambient aqueous conditions. The approach we outline with artificial protein scaffolds has the potential to develop into a toolkit of novel additives for wider nanomaterial fabrication.

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