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Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis

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 bindi...

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Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5949846/
https://www.ncbi.nlm.nih.gov/pubmed/29861896
http://dx.doi.org/10.1039/c5sc01472g
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author 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.
author_facet 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.
author_sort Rawlings, Andrea E.
collection PubMed
description 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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spelling pubmed-59498462018-06-01 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. Chem Sci Chemistry 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. Royal Society of Chemistry 2015-10-01 2015-06-30 /pmc/articles/PMC5949846/ /pubmed/29861896 http://dx.doi.org/10.1039/c5sc01472g Text en This journal is © The Royal Society of Chemistry 2015 http://creativecommons.org/licenses/by-nc/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported Licence (CC BY-NC 3.0)
spellingShingle Chemistry
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
title Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis
title_full Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis
title_fullStr Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis
title_full_unstemmed Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis
title_short Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis
title_sort phage display selected magnetite interacting adhirons for shape controlled nanoparticle synthesis
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5949846/
https://www.ncbi.nlm.nih.gov/pubmed/29861896
http://dx.doi.org/10.1039/c5sc01472g
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