A Metal Organic Framework with Spherical Protein Nodes: Rational Chemical Design of 3D Protein Crystals

Sontz, Pamela A.; Bailey, J.B.; Ahn, Sunhyung; Tezcan, F.A.

doi:10.1021/jacs.5b07463

Cited by 175 publications

(215 citation statements)

References 44 publications

(82 reference statements)

Supporting

Mentioning

208

Contrasting

Unclassified

Order By: Relevance

“…The structural details for the accumulation of Pd ions or Pd(allyl) complexes into the ferritin cage were also reported1633. The structures indicated that the three-fold symmetric channels of the cage are used for accumulation of a number of metal ions16263435. It is expected that such pre-organized metal ions in the narrow channel of ferritin can be converted to a single sub-nanocluster by reduction reaction because the unique coordination environment in the confined protein cavity stabilizes the intermediate structures with flexible amino-acid residues, as previously described in the literatures1012.…”

mentioning

confidence: 95%

Observation of gold sub-nanocluster nucleation within a crystalline protein cage

2017

View full text Add to dashboard Cite

Protein scaffolds provide unique metal coordination environments that promote biomineralization processes. It is expected that protein scaffolds can be developed to prepare inorganic nanomaterials with important biomedical and material applications. Despite many promising applications, it remains challenging to elucidate the detailed mechanisms of formation of metal nanoparticles in protein environments. In the present work, we describe a crystalline protein cage constructed by crosslinking treatment of a single crystal of apo-ferritin for structural characterization of the formation of sub-nanocluster with reduction reaction. The crystal structure analysis shows the gradual movement of the Au ions towards the centre of the three-fold symmetric channels of the protein cage to form a sub-nanocluster with accompanying significant conformational changes of the amino-acid residues bound to Au ions during the process. These results contribute to our understanding of metal core formation as well as interactions of the metal core with the protein environment.

show abstract

mentioning

confidence: 95%

Observation of gold sub-nanocluster nucleation within a crystalline protein cage

2017

View full text Add to dashboard Cite

show abstract

“…(g) Light‐mediated formation and dissociation of the nanotubular assembly (NT). (h) TEM images of the assembled (left) and monomeric (right) GroEL proteins (Reprinted with permission from Sontz et al (). Copyright 2015 American Chemical Society, Zhang et al ().…”

Section: Self‐assembly and Highly Ordered Protein Materialsmentioning

confidence: 99%

Highly ordered protein cage assemblies: A toolkit for new materials

Korpi

Anaya‐Plaza

Välimäki

et al. 2019

WIREs Nanomed Nanobiotechnol

View full text Add to dashboard Cite

Protein capsids are specialized and versatile natural macromolecules with exceptional properties. Their homogenous, spherical, rod‐like or toroidal geometry, and spatially directed functionalities make them intriguing building blocks for self‐assembled nanostructures. High degrees of functionality and modifiability allow for their assembly via non‐covalent interactions, such as electrostatic and coordination bonding, enabling controlled self‐assembly into higher‐order structures. These assembly processes are sensitive to the molecules used and the surrounding conditions, making it possible to tune the chemical and physical properties of the resultant material and generate multifunctional and environmentally sensitive systems. These materials have numerous potential applications, including catalysis and drug delivery. This article is categorized under: Biology‐Inspired Nanomaterials > Protein and Virus‐Based Structures

show abstract

“…For example, at the three‐fold channel of the ferritin container (Figure ), amino acids were introduced for metal‐ion coordination. Using these ferritin variants as nodes, the linkage of the coordinated metal ions with small organic linkers afforded three‐dimensional materials, reminiscent of metal‐organic frameworks . The structural assembly of these materials can be tuned within certain limits by changing the linker molecules …”

Section: D Materialsmentioning

confidence: 99%

Multi‐Component Self‐Assembly of Proteins and Inorganic Particles: From Discrete Structures to Biomimetic Materials

Künzle

Lach

Beck

2019

Israel Journal of Chemistry

View full text Add to dashboard Cite

Due to their defined structure, proteins are suitable building blocks for the bottom‐up construction of multi‐component materials. Especially protein containers, with their inherent cavity, can be used to encapsulate synthetic components such as inorganic nanoparticles. This way, multi‐component discrete structures can be assembled. With recent advances in computational protein design, novel protein containers were successfully created, with a high potential for application in biomedicine and materials research. Moreover, engineered protein containers offer a unique building block for the self‐assembly of three‐dimensional materials. They combine the molecular precision of proteins with nanoscale dimensions. Designed interactions lead to novel protein scaffolds. In addition, nanoparticles encapsulated inside the container cavity introduce orthogonal functionality, important for the realization of nanostructured biomimetic materials with emergent properties.

show abstract

A Metal Organic Framework with Spherical Protein Nodes: Rational Chemical Design of 3D Protein Crystals

Cited by 175 publications

References 44 publications

Observation of gold sub-nanocluster nucleation within a crystalline protein cage

Observation of gold sub-nanocluster nucleation within a crystalline protein cage

Highly ordered protein cage assemblies: A toolkit for new materials

Multi‐Component Self‐Assembly of Proteins and Inorganic Particles: From Discrete Structures to Biomimetic Materials

Contact Info

Product

Resources

About