scholarly journals Thermophoretic Trap for Single Amyloid Fibril and Protein Aggregation Studies

2019 ◽  
Author(s):  
Frank Cichos ◽  
Martin Fränzl ◽  
Tobias Thalheim ◽  
Juliane Adler ◽  
Daniel Huster ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibril

scholarly journals Biophysical Studies on Protein Aggregation and Amyloid Fibril Formation

2012 ◽  
Vol 102 (3) ◽  
pp. 443a
Author(s):  
Mily Bhattacharya ◽  
Neha Jain ◽  
Priyanka Dogra ◽  
Soumyadyuti Samai ◽  
Smita Patil ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Biophysical Studies

scholarly journals Inhibition of Protein Aggregation by Several Antioxidants

2018 ◽  
Vol 2018 ◽  
pp. 1-12 ◽  
Author(s):  
Samra Hasanbašić ◽  
Alma Jahić ◽  
Selma Berbić ◽  
Magda Tušek Žnidarič ◽  
Eva Žerovnik
Keyword(s):  
Vitamin C ◽  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Transmission Electron ◽  
Tht Fluorescence ◽  
Shared Property ◽  
High Concentrations ◽  
Kinetics Of

Amyloid fibril formation is a shared property of all proteins; therefore, model proteins can be used to study this process. We measured protein aggregation of the model amyloid-forming protein stefin B in the presence and absence of several antioxidants. Amyloid fibril formation by stefin B was routinely induced at pH 5 and 10% TFE, at room temperature. The effects of antioxidants NAC, vitamin C, vitamin E, and the three polyphenols resveratrol, quercetin, and curcumin on the kinetics of fibril formation were followed using ThT fluorescence. Concomitantly, the morphology and amount of the aggregates and fibrils were checked by transmission electron microscopy (TEM). The concentration of the antioxidants was varied, and it was observed that different modes of action apply at low or high concentrations relative to the binding constant. In order to obtain more insight into the possible mode of binding, docking of NAC, vitamin C, and all three polyphenols was done to the monomeric form of stefin B.

Thermophoretic trap for single amyloid fibril and protein aggregation studies

2019 ◽  
Vol 16 (7) ◽  
pp. 611-614 ◽  
Author(s):  
Martin Fränzl ◽  
Tobias Thalheim ◽  
Juliane Adler ◽  
Daniel Huster ◽  
Juliane Posseckardt ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibril

Protein Aggregation and Amyloid Fibril Formation by an SH3 Domain Probed by Limited Proteolysis

2003 ◽  
Vol 334 (1) ◽  
pp. 129-141 ◽  
Author(s):  
Patrizia Polverino de Laureto ◽  
Niccolò Taddei ◽  
Erica Frare ◽  
Cristina Capanni ◽  
Silvia Costantini ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Limited Proteolysis ◽  
Sh3 Domain ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

scholarly journals Citrate stabilized gold nanoparticles interfere with amyloid fibril formation: D76N and ΔN6 β2-microglobulin variants

Nanoscale ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 4793-4806 ◽  
Author(s):  
Giorgia Brancolini ◽  
Maria Celeste Maschio ◽  
Cristina Cantarutti ◽  
Alessandra Corazza ◽  
Federico Fogolari ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Β2 Microglobulin ◽  
Amyloid Fibril Formation

Mechanism for how citrate covered gold NP influence protein aggregation and thus fibril formation for the highly amyloidogenic variants D76N and ΔN6 β2-microglobulin.

scholarly journals Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

2006 ◽  
Vol 39 (2) ◽  
pp. 167-201 ◽  
Author(s):  
Hilal A. Lashuel ◽  
Peter T. Lansbury
Keyword(s):  
Neurodegenerative Diseases ◽  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Common Mechanism ◽  
Spongiform Encephalopathy ◽  
Amyloid Fibril Formation ◽  
Amyloid Diseases

1. Introduction 22. What is the significance of the shared structural properties of disease-associated protein fibrils? 32.1 Mechanism of amyloid fibril formation in vitro 62.1.1 In vitro fibril formation involves transient population of ordered aggregates of intermediate stability, or protofibrils 63. Toxic properties of protofibrils 73.1 Protofibrils, rather than fibrils, are likely to be pathogenic 73.2 The toxic protofibril may be a mixture of related species 83.3 Morphological similarities of protofibrils suggest a common mechanism of toxicity 93.4 Are the amyloid diseases a subset of a much larger class of previously unrecognized protofibril diseases? 93.5 Fibrils, in the form of aggresomes, may function to sequester toxic protofibrils 94. Amyloid pores, a common structural link among protein aggregation neurodegenerative diseases 104.1 Mechanistic studies of amyloid fibril formation reveal common features, including pore-like protofibrils 104.1.1 Amyloid-β (Aβ) (Alzheimer's disease) 104.1.2 α-Synuclein (PD and diffuse Lewy body disease) 124.1.3 ABri (familial British dementia) 134.1.4 Superoxide dismutase-1 (amyotrophic lateral sclerosis) 134.1.5 Prion protein (Creutzfeldt–Jakob disease, bovine spongiform encephalopathy, etc.) 144.1.6 Huntingtin (Huntington's disease) 144.2 Amyloidogenic proteins that are not linked to disease also from pore-like protofibrils 154.3 Amyloid proteins form non-fibrillar aggregates that have properties of protein channels or pores 154.3.1 Aβ ‘channels’ 154.3.2 α-Synuclein ‘pores’ 164.3.3 PrP ‘channels’ 164.3.4 Polyglutamine ‘channels’ 174.4 Nature uses β-strand-mediated protein oligomerization to construct pore-forming toxins 175. Mechanisms of protofibril induced toxicity in protein aggregation diseases 195.1 The amyloid pore can explain the age-association and cell-type selectivity of the neurodegenerative diseases 195.2 Protofibrils may promote their own accumulation by inhibiting the proteasome 206. Testing the amyloid pore hypothesis by attempting to disprove it 217. Acknowledgments 228. References 22Protein fibrillization is implicated in the pathogenesis of most, if not all, age-associated neurodegenerative diseases, but the mechanism(s) by which it triggers neuronal death is unknown. Reductionist in vitro studies suggest that the amyloid protofibril may be the toxic species and that it may amplify itself by inhibiting proteasome-dependent protein degradation. Although its pathogenic target has not been identified, the properties of the protofibril suggest that neurons could be killed by unregulated membrane permeabilization, possibly by a type of protofibril referred to here as the ‘amyloid pore’. The purpose of this review is to summarize the existing supportive circumstantial evidence and to stimulate further studies designed to test the validity of this hypothesis.

The effect of macromolecular crowding on protein aggregation and amyloid fibril formation

2004 ◽  
Vol 17 (5) ◽  
pp. 456-464 ◽  
Author(s):  
Larissa A. Munishkina ◽  
Elisa M. Cooper ◽  
Vladimir N. Uversky ◽  
Anthony L. Fink
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Macromolecular Crowding ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

scholarly journals Role of Pre-molten Globule Structure in Protein Amyloid Fibril Formation

2019 ◽  
Vol 7 (1) ◽  
pp. 35-42
Author(s):  
Ali Es-haghi ◽  
Mahsa Jahedi Moghaddam ◽  
Koorosh Shahpasand
Keyword(s):  
Protein Aggregation ◽  
Protein Unfolding ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Molten Globule ◽  
Critical Event ◽  
Diabetic Mellitus ◽  
Native Conformation ◽  
Amyloid Fibril Formation

The conversion of a protein from its native conformation to the pathogenic form is a critical event in the pathogenesis of several neurodegenerative disorders such as Alzheimer’s (AD), Parkinson’s, and Huntington’s diseases, along with type II diabetic mellitus. Although there are several reports on the mechanism of protein aggregation, the actual conformation playing a part in the pathogenicity is yet unclear. Accordingly, the present study summarizes the early pathogenic conformation resulting in several protein aggregations. It is well-documented that a pre-molten globule (MG) structure appears at the early stages of some proteins. Pre-MG is one of the intermediate structures, which is formed during some protein unfolding processes. In addition, it is shown that the pre-molten structure is more flexible than the mature MG one and thus, protein easily rearranges to form amyloid fibrils in this conformation. Therefore, protein aggregation is halted by preventing the pre-MG structure. The strategy of protein aggregation prevention has profound implications in fighting the devastating disorder.

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