2016
DOI: 10.1038/ncomms11771
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Geometrical assembly of ultrastable protein templates for nanomaterials

Abstract: The fabrication of nanoscale devices requires architectural templates on which to position functional molecules in complex arrangements. Protein scaffolds are particularly promising templates for nanomaterials due to inherent molecular recognition and self-assembly capabilities combined with genetically encoded functionalities. However, difficulties in engineering protein quaternary structure into stable and well-ordered shapes have hampered progress. Here we report the development of an ultrastable biomolecul… Show more

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Cited by 41 publications
(65 citation statements)
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References 31 publications
(55 reference statements)
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“…Furthermore, the addition of a trimerization domain into one of the engineered subunits enabled the creation of a three-way connector that assembles with filaments containing the opposing helical sequence into geometrically ordered shapes such as pinwheels ( Figure 1 ). These protein shapes were ideal templates for building nanomaterials that included highly conductive nanowires, 36 and demonstrate that the calligraphy of proteins is maturing beyond the proof of principle stage and moving toward application in solving a host of challenging problems.…”
Section: Scripting Novel Protein Nanostructuresmentioning
confidence: 98%
See 1 more Smart Citation
“…Furthermore, the addition of a trimerization domain into one of the engineered subunits enabled the creation of a three-way connector that assembles with filaments containing the opposing helical sequence into geometrically ordered shapes such as pinwheels ( Figure 1 ). These protein shapes were ideal templates for building nanomaterials that included highly conductive nanowires, 36 and demonstrate that the calligraphy of proteins is maturing beyond the proof of principle stage and moving toward application in solving a host of challenging problems.…”
Section: Scripting Novel Protein Nanostructuresmentioning
confidence: 98%
“… 35 Our recent paper demonstrated that the natural protein–protein interface of a filamentous protein can be redesigned using coiled coils to impart specificity and drive filament assembly into multifaceted structures. 36 In this approach, modular connector proteins were created by replacing one of the two contact interfaces in the filament subunit with opposing helical domains that associate together as tight heterodimeric coiled coils ( Figure 2 B). The resulting pair of connector proteins bound to each other with high specificity while also incorporating into nascent filaments.…”
Section: Scripting Novel Protein Nanostructuresmentioning
confidence: 99%
“…A recent contribution by Clark et al [54] offers a promising “ultrastable biomolecular construction kit for the assembly of filamentous proteins into geometrically defined templates of controllable size and symmetry”. The kit is based on the filamentous protein γ-prefoldin derived from the hyperthermophile Methanocaldococcus jannaschii , and its use as the major component of a biotemplate has been constructed in combination with other protein-made connecting units (see also Slocik et al [45]).…”
Section: Protein-made Fibers and Tubes As Biotemplatesmentioning
confidence: 99%
“…The naturally filament-forming protein γ-prefoldin has been used to engineer self-assembling protein filaments that can be functionalized. [33] Impressive examples of non-fibrous protein-based materials have been engineered recently. [34][35][36] Here, a flexible alternative for engineering protein fibril-based nanoscale scaffolds under mild conditions, based on β-solenoid protein (BSPs), is discussed.…”
Section: Introductionmentioning
confidence: 99%