Cytochrome Display on Amyloid Fibrils

Baldwin, Andrew J.; Bader, Reto; Christodoulou, John; MacPhee, Cait E.; Dobson, Christopher M.; Barker, Paul D.

doi:10.1021/ja0565673

Cited by 150 publications

(155 citation statements)

References 12 publications

Supporting

Mentioning

154

Contrasting

Unclassified

Order By: Relevance

“…The followed simulation protocol and convergence criteria are the same as described in Ref. 24, which uses the CHARMM19 38 polar force field in conjunction with an effective Gaussian model for water 39 ,…”

Section: Adhesion Energy Calculation From Atomistic Simulationsmentioning

confidence: 99%

“…There are examples of amyloids used as bionanomaterials in the form of nanowires 10,[17][18][19] , scaffolds and (bio)templates 10,[20][21][22][23][24][25] , liquid crystals 26 , adhesives 27 and films 14 . This wide range of applications is justified by the amyloid's remarkable mechanical and thermal stability and by their chemical properties that can be tuned via the introduction of additional elements, including enzymes, metal ions, fluorophores, biotin or cytochromes.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Self-folding and aggregation of amyloid nanofibrils

2011

View full text Add to dashboard Cite

Amyloids are highly organized protein filaments, rich in beta-sheet secondary structures that self-assemble to form dense plaques in brain tissues affected by severe neurodegenerative disorders (e.g. Alzheimer's Disease). Identified as natural functional materials in bacteria, in addition to their remarkable mechanical properties, amyloids have also been proposed as a platform for novel biomaterials in nanotechnology applications including nanowires, liquid crystals, scaffolds and thin films. Despite recent progress in the understanding amyloid structure and behavior, the latent selfassembly mechanism and the underlying adhesion forces that drive the aggregation process remain poorly understood. On the basis of previous full atomistic simulations, here we report a simple coarse-grain model to analyze the competition between adhesive forces and elastic deformation of amyloid fibrils. We use simple model system to investigate self-assembly mechanisms of fibrils, focused on the formation of self-folded nanorackets and nanorings, and thereby address a critical issue in linking the biochemical (Angstrom) to micrometer scales relevant for larger-scale states of functional amyloid materials. We investigate the effect of varying the interfibril adhesion energy on the structure and stability of self-folded nanorackets and nanorings and demonstrate that such aggregated amyloid fibrils are stable in such states even when the fibril-fibril interaction is relatively weak, suggesting a strong propensity towards aggregation, given that the constituting amyloid fibril lengths exceed a critical fibril length-scale of several hundred nanometers. We further present a simple approach to directly determine the interfibril adhesion strength from geometric measures. In addition to providing insight into the physics of aggregation of amyloid fibrils our model enables the analysis of large-scale amyloid plaques and presents a new method for the estimation and engineering of the adhesive forces responsible of the self-assembly process of amyloid nanostructures, filling a 2 gap that previously existed between full atomistic simulations of primarily ultra-short fibrils and much larger micrometer-scale amyloid aggregates. Via direct simulation of large-scale amyloid plaques consisting of hundreds of fibrils we demonstrate that the fibril length has a profound impact on their structure and mechanical properties, where critical fibril length-scale derived from our analysis defines the structure of amyloid plaques. A multi-scale modeling approach as used here, bridging the scales from Angstroms to micrometers, opens a wide range of possible nanotechnology applications by presenting a holistic framework that balances mechanical properties of individual fibrils, hierarchical self-assembly, and the adhesive forces determining their stability to facilitate the design of de novo amyloid materials.

show abstract

Section: Adhesion Energy Calculation From Atomistic Simulationsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Self-folding and aggregation of amyloid nanofibrils

2011

View full text Add to dashboard Cite

show abstract

“…Amyloid fibrils adorned with bioactive proteins were prepared with yeast prion Ure2 protein (a regulator of nitrogen catabolism) decorated with proteins such as barnase protein, carbonic anhydrase, glutathione S-transferase, and green fluorescent protein (37). The cytochrome b units successfully attached to amyloid fibrils of the SH3 domain allowed for efficient incorporation of heme moieties into functional amyloid fibrils exhibiting long-distance electron transfer (38). Additional effects have been also demonstrated as the fibrils were transformed into liquid crystal and hydrogel states.…”

Section: Amyloidogenesismentioning

confidence: 99%

Mechanism of amyloidogenesis: nucleation-dependent fibrillation versus double-concerted fibrillation

Bhak

Choe²,

Paik

2009

BMB Reports

View full text Add to dashboard Cite

“…As these sophisticated structures can be constructed without special equipment, fibrils made of either natural or artificial proteins have been studied for use in various functional materials [4][5][6] . For example, fibrils have been used as scaffolds for metals 7,8 and functional proteins 9,10 and as networks for tissue engineering applications 11 .…”

mentioning

confidence: 99%

Hyperthin nanochains composed of self-polymerizing protein shackles

et al. 2013

View full text Add to dashboard Cite

Protein fibrils are expected to have applications as functional nanomaterials because of their sophisticated structures; however, nanoscale ordering of the functional units of protein fibrils remains challenging. Here we design a series of self-polymerizing protein monomers, referred to as protein shackles, derived from modified recombinant subunits of pili from Streptococcus pyogenes. The monomers polymerize into nanochains through spontaneous irreversible covalent bond formation. We design the protein shackles so that their reactions can be controlled by altering redox conditions, which affect disulphide bond formation between engineered cysteine residues. The interaction between the monomers improves their polymerization reactivity and determines morphologies of the polymers. In addition, green fluorescent protein-tagged protein shackles can polymerize, indicating proteins can be stably attached to the nanochains with its functionality preserved. Furthermore we demonstrate that a molecular-recognizable nanochain binds to its partner with an enhanced binding ability in solution. These characteristics are expected to be applied for novel protein nanomaterials.

show abstract

Cytochrome Display on Amyloid Fibrils

Cited by 150 publications

References 12 publications

Self-folding and aggregation of amyloid nanofibrils

Self-folding and aggregation of amyloid nanofibrils

Mechanism of amyloidogenesis: nucleation-dependent fibrillation versus double-concerted fibrillation

Hyperthin nanochains composed of self-polymerizing protein shackles

Contact Info

Product

Resources

About