Hierarchical ordering of amyloid fibrils on the mica surface

A common goal across different fields (e.g. separations, biosensors, biomaterials, pharmaceuticals) is to understand how protein behavior at solid-liquid interfaces is affected by environmental conditions. Temperature, pH, ionic strength, and the chemical and physical properties of the solid surface, among many factors, can control microscopic protein dynamics (e.g. adsorption, desorption, diffusion, aggregation) that contribute to macroscopic properties like time-dependent total protein surface coverage and protein structure. These relationships are typically studied through a top-down approach in which macroscopic observations are explained using analytical models that are based upon reasonable, but not universally true, simplifying assumptions about microscopic protein dynamics. Conclusions connecting microscopic dynamics to environmental factors can be heavily biased by potentially incorrect assumptions. In contrast, more complicated models avoid several of the common assumptions but require many parameters that have overlapping effects on predictions of macroscopic, average protein properties. Consequently, these models are poorly suited for the top-down approach. Because the sophistication incorporated into these models may ultimately prove essential to understanding interfacial protein behavior, this article proposes a bottom-up approach in which direct observations of microscopic protein dynamics specify parameters in complicated models, which then generate macroscopic predictions to compare with experiment. In this framework, single-molecule tracking has proven capable of making direct measurements of microscopic protein dynamics, but must be complemented by modeling to combine and extrapolate many independent microscopic observations to the macro-scale. The bottom-up approach is expected to better connect environmental factors to macroscopic protein behavior, thereby guiding rational choices that promote desirable protein behaviors.

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“…These fibrils grow by a mechanism that involves a combination of protein adsorption and conformational changes. [13–16] …”

Section: Microscopic Protein Dynamicsmentioning

confidence: 99%

A bottom-up approach to understanding protein layer formation at solid–liquid interfaces

Kastantin

Langdon

Schwartz

2014

Advances in Colloid and Interface Science

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“…These assemblies differently graft surfaces with opposite wettability with different resistance to harsh washing. The knowledge of self‐assembly mechanism and boundary condition requirements for amyloid aggregation on the surfaces, (Accardo et al, ; Bellucci et al, , ; Du et al, ; Lin et al, ; Moores et al, ; Shaw et al, ; Vácha et al, ; Zhou et al, ) open the way to molecular level design of protein‐based devices for industrial and biomedical applications (Bleem and Daggett, ).…”

Section: Discussionmentioning

confidence: 99%

“…2A). Indeed, it is well known that the physicochemical nature of the surface can affect the size and shape of aggregates and fibrils, as well as the kinetics of their formation (Accardo et al, 2015;Bellucci et al, 2016Bellucci et al, , 2017Du et al, 2015;Lin et al, 2014;Moores et al, 2011;Shaw et al, 2012;V acha et al, 2014;Zhou et al, 2013). Single monomers in solution can only interact with each other; instead they have fewer degrees of freedom in the presence of a surface, depending on the chemical nature of the surface and their interaction with it (Moores et al, 2011(Moores et al, ).…”

Section: Discussionmentioning

confidence: 99%

“…These assemblies differently graft surfaces with opposite wettability with different resistance to harsh washing. The knowledge of self-assembly mechanism and boundary condition requirements for amyloid aggregation on the surfaces, (Accardo et al, 2015;Bellucci et al, 2016Bellucci et al, , 2017Du et al, 2015;Lin et al, 2014;Moores et al, 2011;Shaw et al, 2012;V acha et al, 2014;Zhou et al, 2013) open the way to molecular level design of protein-based devices for industrial and biomedical applications (Bleem and Daggett, 2017). This work was supported by a grant from the Ministero dell'Universit a e della Ricerca Scientifica-Industrial research project "Development of green technologies for the production of BIO-chemicals and their use in the preparation and industrial application of POLImeric materials from agricultural biomasses cultivated in a sustainable way in Campania (BioPoliS)" PON03PE 00107 1, funded within the framework of Operative National Program Research and Competitiveness 2007D.…”

Section: Discussionmentioning

confidence: 99%

“…Despite the fact that all amyloidogenic proteins are different in their native monomeric conformation, their polymerization leads to the same fibrillary structure with a cross b-sheet fold (Biancalana and Koide, 2010;Fowler et al, 2007;Hamley, 2007;Ruggeri et al, 2015). The pathway of formation of mature amyloid fibrils occurs via the hierarchical self-assembly (Ridgley and Barone, 2013;Zhou et al, 2013) of oligomers, metastable structures or protofibrils (Miti et al, 2015) and generally evolves through nucleation and elongation steps (Arosio et al, 2015;W€ ordehoff et al, 2015). However, their formation can result from different environmental conditions (temperature, pH and ionic strength) and, interestingly, can be affected also by the presence of surfaces and interfaces (Accardo et al, 2015;Bellucci et al, 2016Bellucci et al, , 2017Du et al, 2015;Lin et al, 2014;Moores et al, 2011;Shaw et al, 2012;V acha et al, 2014;Zhou et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

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Self‐assembly of two hydrophobins from marine fungi affected by interaction with surfaces

Cicatiello

Dardano

Pirozzi

et al. 2017

Biotech & Bioengineering

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Hydrophobins are amphiphilic fungal proteins endowed with peculiar characteristics, such as a high surface activity and an interface triggered self-assembly. Several applications of these proteins have been proposed in the food, cosmetics and biomedical fields. Moreover, their use as proteinaceous coatings can be effective for materials and nanomaterials applications. The discovery of novel hydrophobins with diverse properties may be advantageous from both the scientific and industrial points of view. Stressful environmental conditions of fungal growth may induce the production of proteins with peculiar features. Two Class I hydrophobins from fungi isolated from marine environment have been recently purified. Herein, their propensity to aggregate forming nanometric fibrillar structures has been compared, using different techniques, such as circular dichroism, dynamic light scattering and Thioflavin T fluorescence assay. Furthermore, TEM and AFM images indicate that the interaction of these proteins with specific surfaces, are crucial in the formation of amyloid fibrils and in the assembly morphologies. These self-assembling proteins show promising properties as bio-coating for different materials via a green process. Biotechnol. Bioeng. 2017;114: 2173-2186. © 2017 Wiley Periodicals, Inc.

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Fibril Film Formation of Pseudoenantiomeric Oxymethylenehelicene Oligomers at the Liquid–Solid Interface: Structural Changes, Aggregation, and Discontinuous Heterogeneous Nucleation

Shigeno

Sawato

Yamaguchi

2015

Chemistry A European J

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Oxymethylenehelicene (P)- and (M)-oligomers up to a nonamer were synthesized by a building block method. The oligomers formed dimeric homoaggregates in trifluoromethylbenzene. A mixture of the pseudoenantiomeric (P)-pentamer and (M)-hexamer formed a heteroaggregate, which self-assembled into one-dimensional fibril films at the liquid-solid interface. Discontinuous heterogeneous nucleation occurred, which involved the formation of particles that were 50 nm in diameter and subsequent fibril growth from these particles. The fibril film was formed on the solid surface and the molecules remained dissociated in solution. The fibril film formation was affected by seeding and the solid surface materials.

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Hierarchical ordering of amyloid fibrils on the mica surface

Cited by 21 publications

References 60 publications

A bottom-up approach to understanding protein layer formation at solid–liquid interfaces

A bottom-up approach to understanding protein layer formation at solid–liquid interfaces

Self‐assembly of two hydrophobins from marine fungi affected by interaction with surfaces

Fibril Film Formation of Pseudoenantiomeric Oxymethylenehelicene Oligomers at the Liquid–Solid Interface: Structural Changes, Aggregation, and Discontinuous Heterogeneous Nucleation

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