Amyloids: From molecular structure to mechanical properties

Schleeger, Michael; vandenAkker, Corianne C.; Deckert‐Gaudig, Tanja; Deckert, Volker; Velikov, Krassimir P.; Koenderink, Gijsje H.; Bonn, Mischa

doi:10.1016/j.polymer.2013.02.029

Cited by 95 publications

(95 citation statements)

References 117 publications

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“…However, the weak point of these zipping experiments is that the measurements were based on nonspecific binding between the tip and the fibrils. Therefore, the variability between individual measurements likely results from random and multiple attachment sites of the protein to the tip [187]. …”

Section: Single Molecule Investigation By Atomic Force Microscopy Tecmentioning

confidence: 99%

AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species

Ruggeri

Habchi

Cerreta

et al. 2016

CPD

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BackgroundA wide class of human diseases and neurodegenerative disorders, such as Alzheimer’s disease, is due to the failure of a specific peptide or protein to keep its native functional conformational state and to undergo a conformational change into a misfolded state, triggering the formation of fibrillar cross-β sheet amyloid aggregates. During the fibrillization, several coexisting species are formed, giving rise to a highly heterogeneous mixture. Despite its fundamental role in biological function and malfunction, the mechanism of protein self-assembly and the fundamental origins of the connection between aggregation, cellular toxicity and the biochemistry of neurodegeneration remains challenging to elucidate in molecular detail. In particular, the nature of the specific state of proteins that is most prone to cause cytotoxicity is not established.Methods:In the present review, we present the latest advances obtained by Atomic Force Microscopy (AFM) based techniques to unravel the biophysical properties of amyloid aggregates at the nanoscale. Unraveling amyloid single species biophysical properties still represents a formidable experimental challenge, mainly because of their nanoscale dimensions and heterogeneous nature. Bulk techniques, such as circular dichroism or infrared spectroscopy, are not able to characterize the heterogeneity and inner properties of amyloid aggregates at the single species level, preventing a profound investigation of the correlation between the biophysical properties and toxicity of the individual species.Conclusion:The information delivered by AFM based techniques could be central to study the aggregation pathway of proteins and to design molecules that could interfere with amyloid aggregation delaying the onset of misfolding diseases.

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Section: Single Molecule Investigation By Atomic Force Microscopy Tecmentioning

confidence: 99%

AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species

Ruggeri

Habchi

Cerreta

et al. 2016

CPD

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“…Amyloid fibrils are known to display impressive material properties, including high deformation resistance, elasticity, and persistence under extreme conditions. Insulin fibrils, for example, exhibit an ultimate strength of 0.6 ± 0.4 GPa, comparable to that of steel, and a Young's modulus of 3.3 ± 0.4 GPa, similar to that of silk (Schleeger et al, ; Smith et al, ). In nature, these remarkable characteristics have been harnessed by countless organisms to serve a wide variety of purposes (Table and Fig.…”

Section: Functional Amyloidsmentioning

confidence: 99%

Structural and functional diversity among amyloid proteins: Agents of disease, building blocks of biology, and implications for molecular engineering

Bleem

Daggett

2016

Biotech & Bioengineering

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Amyloids have long been associated with protein dysfunction and neurodegenerative diseases, but recent research has demonstrated that some organisms utilize the unique properties of the amyloid fold to create functional structures with important roles in biological processes. Additionally, new engineering approaches have taken advantage of amyloid structures for implementation in a wide variety of materials and devices. In this review, the role of amyloid in human disease is discussed and compared to the functional amyloids, which serve a largely structural purpose. We then consider the use of amyloid constructs in engineering applications, including their utility as building blocks for synthetic biology and molecular engineering. Biotechnol. Bioeng. 2017;114: 7-20. © 2016 Wiley Periodicals, Inc.

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“…As shown in Figure , peptides can self‐assemble to form nanofibrils using a variety of monomers . Oligopeptides or polypeptides molecules first form β‐sheet structures due to the interaction between alternating hydrophilic and hydrophobic amino acids in their chains and then thin and long fibrils typically form from two or more twisted strands . Usually lyophilized peptide monomers are dissolved in water and incubated at a certain temperature and pH to produce nanofibrils.…”

Section: Peptide Nanofibrilsmentioning

confidence: 99%

Peptide nanostructures in biomedical technology

Feyzizarnagh

Yoon

Goltz

et al. 2016

WIREs Nanomed Nanobiotechnol

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Nanostructures of peptides have been investigated for biomedical applications due to their unique mechanical and electrical properties in addition to their excellent biocompatibility. Peptides may form fibrils, spheres and tubes in nanoscale depending on the formation conditions. These peptide nanostructures can be used in electrical, medical, dental, and environmental applications. Applications of these nanostructures include, but are not limited to, electronic devices, biosensing, medical imaging and diagnosis, drug delivery, tissue engineering and stem cell research. This review offers a discussion of basic synthesis methods, properties and application of these nanomaterials. The review concludes with recommendations and future directions for peptide nanostructures. WIREs Nanomed Nanobiotechnol 2016, 8:730-743. doi: 10.1002/wnan.1393 For further resources related to this article, please visit the WIREs website.

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Amyloids: From molecular structure to mechanical properties

Cited by 95 publications

References 117 publications

AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species

AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species

Structural and functional diversity among amyloid proteins: Agents of disease, building blocks of biology, and implications for molecular engineering

Peptide nanostructures in biomedical technology

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