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Amyloid Fibrils from Hemoglobin [PDF]
Biomolecules, 2017 Amyloid fibrils are a class of insoluble protein nanofibers that are formed via the self-assembly of a wide range of peptides and proteins. They are increasingly exploited for a broad range of applications in bionanotechnology, such as biosensing and ...
Nadishka Jayawardena +7 more
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Pathway Dependence of the Formation and Development of Prefibrillar Aggregates in Insulin B Chain
Molecules, 2022 Amyloid fibrils have been an important subject as they are involved in the development of many amyloidoses and neurodegenerative diseases. The formation of amyloid fibrils is typically initiated by nucleation, whereas its exact mechanisms are largely ...
Yuki Yoshikawa +10 more
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Endocytosed 2-Microglobulin Amyloid Fibrils Induce Necrosis and Apoptosis of Rabbit Synovial Fibroblasts by Disrupting Endosomal/Lysosomal Membranes: A Novel Mechanism on the Cytotoxicity of Amyloid Fibrils. [PDF]
PLoS ONE, 2015 Dialysis-related amyloidosis is a major complication in long-term hemodialysis patients. In dialysis-related amyloidosis, β2-microglobulin (β2-m) amyloid fibrils deposit in the osteoarticular tissue, leading to carpal tunnel syndrome and destructive ...
Tadakazu Okoshi +4 more
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AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
Nature Communications, 2021 Systemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed ...
Akanksha Bansal +8 more
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Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D Sheets
Biomolecules, 2023 The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human disorders, including many neurodegenerative diseases.
Kanchana Karunarathne +7 more
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Small molecule targeting amyloid fibrils inhibits Streptococcus mutans biofilm formation
AMB Express, 2021 Amyloid fibrils are important scaffold in bacterial biofilms. Streptococcus mutans is an established cariogenic bacteria dwelling within biofilms, and C123 segment of P1 protein is known to form amyloid fibrils in S.
Yuanyuan Chen +4 more
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Amyloid Fibril Solubility [PDF]
The Journal of Physical Chemistry B, 2015 It is well established that amyloid fibril solubility is protein specific, but how solubility depends on the interactions between the fibril building blocks is not clear. Here we use a simple protein model and perform Monte Carlo simulations to directly measure the solubility of amyloid fibrils as a function of the interaction between the fibril ...
Rizzi, LG, Auer, S
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Light Chain Amyloid Fibrils Cause Metabolic Dysfunction in Human Cardiomyocytes. [PDF]
PLoS ONE, 2015 Light chain (AL) amyloidosis is the most common form of systemic amyloid disease, and cardiomyopathy is a dire consequence, resulting in an extremely poor prognosis.
Helen P McWilliams-Koeppen +12 more
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Plasticity of Amyloid Fibrils [PDF]
Biochemistry, 2006 In experiments designed to characterize the basis of amyloid fibril stability through mutational analysis of the Abeta (1-40) molecule, fibrils exhibit consistent, significant structural malleability. In these results, and in other properties, amyloid fibrils appear to more resemble plastic materials generated from synthetic polymers than globular ...
Ronald, Wetzel +2 more
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Nucleation of amyloid fibrils [PDF]
The Journal of Chemical Physics, 2010 We consider nucleation of amyloid fibrils in the case when the process occurs by the mechanism of direct polymerization of practically fully extended protein segments, i.e., β-strands, into β-sheets. Applying the classical nucleation theory, we derive a general expression for the work to form a nanosized amyloid fibril (protofilament) constituted of ...
Kashchiev, Dimo, Auer, Stefan
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