Engineering Amyloid Fibrils from β-Solenoid Proteins for Biomaterials Applications

Peralta, Maria D R; Karsai, Árpád; Ngo, Alice; Sierra, Catherine; Fong, K.; Hayre, Natha Robert; Mirzaee, Nima; Ravikumar, Krishnakumar M.; Kluber, Alexander; Chen, Xi; Liu, Gang-yu; Toney, Michael D.; Singh, Rajiv R. P.; Cox, D. L.

doi:10.1021/nn5056089

Cited by 58 publications

(80 citation statements)

References 70 publications

(111 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…24 The main challenge facing the field of protein nanotechnology is the ability to control proteinprotein interactions to build up higher order structures, and in particular to order these structures. Previous work on creating protein assemblies has been largely centered around amyloid fibers [25][26][27][28][29] but has recently also involved native protein structures [30][31][32] with ring shaped proteins emerging as a commonly used self-assembling feature. [33][34][35][36][37] Recent work has established methods to post functionalize assembled structures, 38,39 an important step towards applications based on protein nanostructures.…”

Section: Introductionmentioning

confidence: 99%

Protein nanorings organized by poly(styrene-block-ethylene oxide) self-assembled thin films

et al. 2015

View full text Add to dashboard Cite

This study explores the use of block copolymer self-assembly to organize Lsmα, a protein which forms stable doughnut-shaped heptameric structures. Here, we have explored the idea that 2-D crystalline arrays of protein filaments can be prepared by stacking doughnut shaped Lsmα protein into the poly(ethylene oxide) blocks of a hexagonal microphase-separated polystyrene-b-polyethylene oxide (PS-b-PEO) block copolymer. We were able to demonstrate the coordinated assembly of such a complex hierarchical nanostructure. The key to success was the choice of solvent systems and protein functionalization that achieved sufficient compatibility whilst still promoting assembly. Unambiguous characterisation of these structures is difficult; however AFM and TEM measurements confirmed that the protein was sequestered into the PEO blocks. The use of a protein that assembles into stackable doughnuts offers the possibility of assembling nanoscale optical, magnetic and electronic structures. This study explores the use of block copolymer self-assembly to organize Lsmα, a protein which forms stable doughnut-shaped heptameric structures. Here, we have explored the idea that 2-D crystalline arrays of protein filaments can be prepared by stacking doughnut shaped Lsmα protein into the poly(ethylene oxide) blocks of a hexagonal microphase-separated polystyrene-b-polyethylene oxide (PSb-PEO) block copolymer. We were able to demonstrate the coordinated assembly of such a complex hierarchical nanostructure. The key to success was the choice of solvent systems and protein functionalization that achieved sufficient compatibility whilst still promoting assembly. Unambiguous characterisation of these structures is difficult; however AFM and TEM measurements confirmed that the protein was sequestered into the PEO blocks. The use of a protein that assembles into stackable doughnuts offers the possibility of assembling nanoscale optical, magnetic and electronic structures.

show abstract

Section: Introductionmentioning

confidence: 99%

Protein nanorings organized by poly(styrene-block-ethylene oxide) self-assembled thin films

et al. 2015

View full text Add to dashboard Cite

show abstract

“…10 We used equilibrium umbrella sampling molecular dynamics simulations to measure both the bending and torsional elastic moduli. By using beam theory, we extend our results for monomers to fibrils to predict persistence lengths for twisting and bending, which generally exceed the micron scale, indicating significant mechanical strength.…”

mentioning

confidence: 99%

“…BSP2 and BSP3 are the previously used spruce budworm (SBAFP) and ryegrass (RGAFP) antifreeze proteins, respectively 10. Images were rendered using VMD 28Nano LettersLetter DOI: 10.1021/nl5049719 Nano Lett.…”

mentioning

confidence: 99%

In Silico Measurements of Twist and Bend Moduli for β-Solenoid Protein Self-Assembly Units

2015

View full text Add to dashboard Cite

We compute potentials of mean force for bend and twist deformations via force pulling and umbrella sampling experiments for four β-solenoid proteins (BSPs) that show promise in nanotechnology applications. In all cases, we find quasi-Hooke's law behavior until the point of rupture. Bending moduli show modest anisotropy for two-sided and three-sided BSPs, and little anisotropy for a four-sided BSP. There is a slight clockwise/counterclockwise asymmetry in the twist potential of mean force, showing greater stiffness when the applied twist follows the intrinsic twist. When we extrapolate to beam theory appropriate for amyloid fibrils of the BSPs, we find bend/twist moduli which are somewhat smaller than those in the literature for other amyloid fibrils. Twist persistence lengths are on the order of a micron, and bend persistence lengths are several microns. Provided the intrinsic twist can be reversed, these results support the usage of BSPs in biomaterials applications.

show abstract

“…Elongation of amyloid fibrils along the fibril axis is related to the binding features of the seed amyloids and their structural stabilities. The binding sites on monomers enable the attachment of other monomers [39]. The specific interactions can be classified as intra-layer interactions and interlayer interactions, which confer structural stability, as depicted in Figure 4.…”

Section: Cross-seeded Fibrilsmentioning

confidence: 99%

Structure-Property Relationship of Amyloidogenic Prion Nanofibrils

Lee¹,

Choi²,

Kim³

et al. 2017

Prion - An Overview

View full text Add to dashboard Cite

The structure and its property for the prion nanofibrils, which exhibit self-assembled steric zipper, amyloid fibrils, are described in this chapter. There is the belief of origin for the infectiousness of the prion can be its molecular structure. It is due to the amyloid toxicity, which is related to its beta sheet rich molecular structure and self-aggregated long fibrils. There is evidence that the difference between PrP c and PrP sc is transitioned beta sheet from alpha helix to self-assemble and then to the amyloidogenic fibrils. Therefore, the scope of this chapter is the amyloidogenic structural characteristics of prion fibrils and its relationship to the property. The molecular structural characteristics can be changed by properties such as affinity, toxicity, infectivity, and so on, so this is a key factor to understand the origin of prion disease and develop the therapeutic strategy. One of the main properties of amyloid fibrils that we want to describe here is mechanical property such as dynamic property and material property for prion nanofibrils. This chapter can shed light on understanding the infectious characteristics of prion and the relationship of its molecular structures.

show abstract

Engineering Amyloid Fibrils from β-Solenoid Proteins for Biomaterials Applications

Cited by 58 publications

References 70 publications

Protein nanorings organized by poly(styrene-block-ethylene oxide) self-assembled thin films

Protein nanorings organized by poly(styrene-block-ethylene oxide) self-assembled thin films

In Silico Measurements of Twist and Bend Moduli for β-Solenoid Protein Self-Assembly Units

Structure-Property Relationship of Amyloidogenic Prion Nanofibrils

Contact Info

Product

Resources

About