From Metal Binding to Nanoparticle Formation: Monitoring Biomimetic Iron Oxide Synthesis within Protein Cages using Mass Spectrometry

Kang, Sebyung; Jolley, Craig C.; Liepold, Lars; Young, Mark; Douglas, Trevor

doi:10.1002/anie.200900437

Cited by 28 publications

(28 citation statements)

References 22 publications

(25 reference statements)

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“…Therefore, the Dps –encapsulated nanoparticles including Co(O)OH and Co 3 O 4 [66], γ-Fe 2 O 3 [67, 68], CdS[69] and Pt[70] have been synthesized using conceptually the same approach as that of ferritins. However, the resulting-nanoparticles are extremely small as Dps proteins have smaller interior cavity of 5nm than that of 8nm in ferritins.…”

Section: Biomedical Technological and Catalytic Applications Of Ferrmentioning

confidence: 99%

“…In addition to protein only macromolecular complexes, it has been demonstrated that interactions between protein macromolecules and metal ions or nanoclusters can be preserved, allowing metal deposition to be monitored by tracking mass increases. [68, 70] Mass spectrometry has sufficient mass accuracy and resolution to discriminate two to three metal ions depending on the atomic masses of metal ions. Therefore, it is possible to concurrently detect multiple populations distributed within an ensemble and monitor their changes individually instead of averaging over all signals.…”

Section: Nanoparticle Assembly (Growth) Protein Cage Assembly and Jamentioning

confidence: 99%

See 1 more Smart Citation

The ferritin superfamily: Supramolecular templates for materials synthesis

Uchida

Kang

Reichhardt

et al. 2010

Biochimica et Biophysica Acta (BBA) - General Subjects

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219

204

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Members of the ferritin superfamily are multi-subunit cage-like proteins with a hollow interior cavity. These proteins possess three distinct surfaces, i.e. interior and exterior surfaces of the cages and interface between subunits. The interior cavity provides a unique reaction environment in which the interior reaction is separated from the external environment. In biology the cavity is utilized for sequestration of irons and biomineralization as a mechanism to render Fe inert and sequester it from the external environment. Material scientists have been inspired by this system and exploited a range of ferritin superfamily proteins as supramolecular templates to encapsulate nanoparticles and/or as well-defined building blocks for fabrication of higher order assembly. Besides the interior cavity, the exterior surface of the protein cages can be modified without altering the interior characteristics. This allows us to deliver the protein cages to a targeted tissue in vivo or to achieve controlled assembly on a solid substrate to fabricate higher order structures. Furthermore, the interface between subunits is utilized for manipulating chimeric self-assembly of the protein cages and in the generation of symmetry-broken Janus particles. Utilizing these ideas, the ferritin superfamily has been exploited for development of a broad range of materials with applications from biomedicine to electronics.

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Section: Biomedical Technological and Catalytic Applications Of Ferrmentioning

confidence: 99%

Section: Nanoparticle Assembly (Growth) Protein Cage Assembly and Jamentioning

confidence: 99%

The ferritin superfamily: Supramolecular templates for materials synthesis

Uchida

Kang

Reichhardt

et al. 2010

Biochimica et Biophysica Acta (BBA) - General Subjects

Self Cite

219

204

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“…In addition, properties such as magnetic response or bandgap energy are often dependent on the crystalline domain size of a sample. In protein-templated nanoparticle synthesis, the size of nanoparticles can often be controlled by tuning the metal ion/protein cage ratio – this results in a fairly narrow distribution of sizes with a mean value that can be easily controlled during synthesis 19 . The feasibility of technological applications of protein-templated nanoparticles will depend largely on our ability to exert synthetic control over material properties beyond the average particle size, such as the typical crystalline domain size within a nanoparticle.…”

Section: Introductionmentioning

confidence: 99%

Size and Crystallinity in Protein-Templated Inorganic Nanoparticles

Jolley

Uchida²,

Reichhardt³

et al. 2010

Chem. Mater.

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Protein cages such as ferritins and virus capsids have been used as containers to synthesize a wide variety of protein-templated inorganic nanoparticles. While identification of the inorganic crystal phase has been successful in some cases, very little is known about the detailed nanoscale structure of the inorganic component. We have used pair distribution function analysis of total X-ray scattering to measure the crystalline domain size in nanoparticles of ferrihydrite, γ-Fe2O3, Mn3O4, CoPt, and FePt grown inside 24-meric ferritin cages from H. sapiens and P. furiosus. The material properties of these protein-templated nanoparticles are influenced by processes at a variety of length scales: the chemistry of the material determines the precise arrangement of atoms at very short distances, while the interior volume of the protein cage constrains the maximum nanoparticle size attainable. At intermediate length scales, the size of coherent crystalline domains appears to be constrained by the arrangement of crystal nucleation sites on the interior of the cage. Based on these observations, some potential synthetic strategies for the control of crystalline domain size in protein-templated nanoparticles are suggested.

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“…Weiterhin wurde die Struktur der beiden Intermediate mit IMMS ermittelt, sowohl von den intakten als auch von den CID-fragmentierten Spezies. [181] Beide [183][184][185] Dendrimere, die kovalent an die Innenseite eines Proteinkäfigs gebunden sind, kçnnen zu nachfolgenden Generationen herangezogen werden. Dabei kçnnen die Partikel ihre Stabilität erhçhen und damit eine Anwendung unter extremeren Bedingungen ermçglichen.…”

Section: Massenanalyse Von Intakten Viralen Aggregatenunclassified

Moderne biomolekulare Massenspektrometrie und ihre Bedeutung für die Erforschung der Struktur, der Dynamik und des Aufbaus von Viren

Uetrecht

Heck

2011

Angewandte Chemie

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Entwickelt vor über einem Jahrhundert und beliebter denn je, findet die Massenspektrometrie als analytisches Verfahren heute in beinahe allen Bereichen der Naturwissenschaften Anwendung. Entwicklungen in den letzten beiden Jahrzehnten ermöglichten die Erforschung von Proteinen, sogar intakten Proteinkomplexen, und eine ernsthafte Nutzung in der Strukturbiologie. In diesem Aufsatz beschreiben wir die wachsende Bedeutung der Massenspektrometrie und ihrer technischen Spielarten für die Strukturbiologie anhand einer ausführlichen Betrachtung der strukturellen Virologie. Wir gehen auf die Entwicklung der Massenspektrometrie zu einem Werkzeug ein, das einzigartige Informationen über Struktur, Konformation, Topologie, Aufbau und Funktion von viralen Protein(komplex)en liefern kann, was schließlich in der direkten Analyse von intakten Viruskapsiden mit einer Masse von mehreren Millionen Dalton gipfelt. Die Massenspektrometrie wird heute zur Bearbeitung weitreichender Fragen der Virologie genutzt und hilft so z. B. zu klären, wie Viren aufgebaut werden und wie sie mit ihrem spezifischen Wirt interagieren.

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From Metal Binding to Nanoparticle Formation: Monitoring Biomimetic Iron Oxide Synthesis within Protein Cages using Mass Spectrometry

Cited by 28 publications

References 22 publications

The ferritin superfamily: Supramolecular templates for materials synthesis

The ferritin superfamily: Supramolecular templates for materials synthesis

Size and Crystallinity in Protein-Templated Inorganic Nanoparticles

Moderne biomolekulare Massenspektrometrie und ihre Bedeutung für die Erforschung der Struktur, der Dynamik und des Aufbaus von Viren

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