The Nucleation of Protein Aggregates - From Crystals to Amyloid Fibrils

2017 ◽  
pp. 187-226 ◽  
Author(s):  
Alexander K. Buell
Keyword(s):  
Amyloid Fibrils ◽  
Protein Aggregates

Dynamics and Fluidity of Amyloid Fibrils:  A Model of Fibrous Protein Aggregates

2002 ◽  
Vol 124 (51) ◽  
pp. 15150-15151 ◽  
Author(s):  
Ami S. Lakdawala ◽  
David M. Morgan ◽  
Dennis C. Liotta ◽  
David G. Lynn ◽  
James P. Snyder
Keyword(s):  
Amyloid Fibrils ◽  
Protein Aggregates ◽  
Fibrous Protein

scholarly journals RETRACTED: Peptide-induced formation of protein aggregates and amyloid fibrils in human and guinea pig αA-crystallins under physiological conditions of temperature and pH

2019 ◽  
Vol 179 ◽  
pp. 193-205 ◽  
Author(s):  
Anbarasu Kumarasamy ◽  
Sivakumar Jeyarajan ◽  
Jonathan Cheon ◽  
Anthony Premceski ◽  
Eric Seidel ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Amyloid Fibrils ◽  
Protein Aggregates ◽  
Physiological Conditions

Is DAPI assay of cellular nucleic acid reliable in the presence of protein aggregates?

2020 ◽  
Vol 56 (89) ◽  
pp. 13844-13847
Author(s):  
Aruna K. Mora ◽  
Sufiyan Khan ◽  
Birija S. Patro ◽  
Sukhendu Nath
Keyword(s):  
Nucleic Acid ◽  
Amyloid Fibrils ◽  
Protein Aggregates

Intracellular amyloid fibrils prevent exclusive staining of nuclei by DAPI.

scholarly journals Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways

FEBS Journal ◽  
2008 ◽  
Vol 275 (9) ◽  
pp. 2021-2031 ◽  
Author(s):  
Driss El Moustaine ◽  
Veronique Perrier ◽  
Laszlo Smeller ◽  
Reinhard Lange ◽  
Joan Torrent
Keyword(s):  
Prion Protein ◽  
Amyloid Fibrils ◽  
Protein Aggregates ◽  
Full Length ◽  
Spherical Particles

scholarly journals Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers

2021 ◽  
Author(s):  
Qiuye Li ◽  
Christopher P. Jaroniec ◽  
Witold K. Surewicz
Keyword(s):  
High Resolution ◽  
Prion Protein ◽  
Prion Disease ◽  
Amyloid Fibrils ◽  
Prion Diseases ◽  
Protein Aggregates ◽  
Direct Support ◽  
Human Prion Protein ◽  
Structural Insight

One of the least understood aspects of prion diseases is the structure of infectious prion protein aggregates. Here we report a high-resolution cryo-EM structure of amyloid fibrils formed by human prion protein with Y145Stop mutation that is associated with a familial prion disease. This structural insight allows us not only to explain previous biochemical findings, but also provides direct support for the conformational adaptability model of prion transmissibility barriers.

scholarly journals Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation

2021 ◽  
Vol 22 (4) ◽  
pp. 1775
Author(s):  
Mantas Ziaunys ◽  
Andrius Sakalauskas ◽  
Tomas Sneideris ◽  
Vytautas Smirnovas
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibrils ◽  
Protein Aggregates ◽  
Amyloid Aggregation ◽  
Amyloid Aggregates ◽  
Affected Tissue ◽  
New Ideas

Protein aggregation into amyloid fibrils is linked to multiple disorders. The understanding of how natively non-harmful proteins convert to these highly cytotoxic amyloid aggregates is still not sufficient, with new ideas and hypotheses being presented each year. Recently it has been shown that more than one type of protein aggregates may co-exist in the affected tissue of patients suffering from amyloid-related disorders, sparking the idea that amyloid aggregates formed by one protein may induce another protein’s fibrillization. In this work, we examine the effect that lysozyme fibrils have on insulin amyloid aggregation. We show that not only do lysozyme fibrils affect insulin nucleation, but they also alter the mechanism of its aggregation.

scholarly journals Synthesis, spectral and luminescent properties of new alkylamino-beta-ketoenol compounds and metal complexes on their basis for creation of fluorescent probes for biomolecules and optical materials

2021 ◽  
pp. 53-64
Author(s):  
Vasyl I. Pekhnyo ◽  
◽  
Viktor Y. Chernii ◽  
Vladyslava B. Kovalska ◽  
Mykhaylo Yu. Losytskyy ◽  
...  
Keyword(s):  
Fluorescent Probes ◽  
Amyloid Fibrils ◽  
Luminescent Properties ◽  
Protein Aggregates ◽  
Fluorescent Detection ◽  
Yellow Emission ◽  
Native Proteins ◽  
Dehydroacetic Acid ◽  
Effective Compound

A series of chalcones and alkylamino-β-ketoenol dyes based on dehydroacetic acid were synthesized in this work. Their individuality is established and physicochemical properties are investigated. A number of phthalocyanine complexes of zirconium and hafnium with these β-ketoenol ligands have been obtained, and their spectral-luminescent properties have been studied. It is established that the obtained complexes absorbs light in a wide spectral range from 300 to 700 nm. Functionalized alkylamino-β-ketoenoles are reported as probes for fluorescent detection of protein aggregates that associated with dangerous diseases, including neurodegenerative disorders. Depending on the nature of the substituents, these dyes can increase the fluorescence intensity tenfold in the presence of fibrillar aggregates, but are practically insensitive to native proteins. The studied dyes have a green-yellow emission in the region of 495–540 nm. For the most effective compound (2E,5Z,7E)-8-(4-(dimethylamino)phenyl)-6-hydroxy-2-(2-methoxyethyl-amino)octa-2,5,7-trien-4-one the fluorescence quantum yield upon binding to insulin fibrils reaches 47.0%, while for the free dye this value is about 0.5%. Due to its sensing properties, this dye exceeds the properties of Thioflavin T, which is the standard for the determination of amyloid fibrils. Alkylamino-β-ketoenol dyes have been shown to be promising as fluorescent probes for the detection of β-pleated protein aggregates.

Sign in / Sign up

Export Citation Format

Share Document