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 Atomic Force Microscopy on Biological Materials Related to Pathological Conditions

Scanning ◽  
2019 ◽  
Vol 2019 ◽  
pp. 1-25 ◽  
Author(s):  
Andreas Stylianou ◽  
Stylianos-Vasileios Kontomaris ◽  
Colin Grant ◽  
Eleni Alexandratou
Keyword(s):  
Atomic Force Microscopy ◽  
High Resolution ◽  
Surface Characterization ◽  
Amyloid Fibrils ◽  
Biological Materials ◽  
Force Microscopy ◽  
Fibrous Protein ◽  
Atomic Force ◽  
Pathological Conditions ◽  
Wide Range

Atomic force microscopy (AFM) is an easy-to-use, powerful, high-resolution microscope that allows the user to image any surface and under any aqueous condition. AFM has been used in the investigation of the structural and mechanical properties of a wide range of biological matters including biomolecules, biomaterials, cells, and tissues. It provides the capacity to acquire high-resolution images of biosamples at the nanoscale and allows at readily carrying out mechanical characterization. The capacity of AFM to image and interact with surfaces, under physiologically relevant conditions, is of great importance for realistic and accurate medical and pharmaceutical applications. The aim of this paper is to review recent trends of the use of AFM on biological materials related to health and sickness. First, we present AFM components and its different imaging modes and we continue with combined imaging and coupled AFM systems. Then, we discuss the use of AFM to nanocharacterize collagen, the major fibrous protein of the human body, which has been correlated with many pathological conditions. In the next section, AFM nanolevel surface characterization as a tool to detect possible pathological conditions such as osteoarthritis and cancer is presented. Finally, we demonstrate the use of AFM for studying other pathological conditions, such as Alzheimer’s disease and human immunodeficiency virus (HIV), through the investigation of amyloid fibrils and viruses, respectively. Consequently, AFM stands out as the ideal research instrument for exploring the detection of pathological conditions even at very early stages, making it very attractive in the area of bio- and nanomedicine.

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 Characterization of Inter- and Intramolecular Interactions of Amyloid Fibrils by AFM-Based Single-Molecule Force Spectroscopy

2016 ◽  
Vol 2016 ◽  
pp. 1-18 ◽  
Author(s):  
Yinli Li ◽  
Hao Liang ◽  
Huiling Zhao ◽  
Dong Chen ◽  
Bo Liu ◽  
...  
Keyword(s):  
Single Molecule ◽  
Self Assembly ◽  
Amyloid Fibrils ◽  
Force Measurement ◽  
Force Spectroscopy ◽  
Structural Features ◽  
Intramolecular Interactions ◽  
Assembly Process ◽  
Fibrous Protein ◽  
Abnormal Accumulation

Amyloids are fibrous protein aggregates defined by shared specific structural features. Abnormal accumulation of amyloid in organs leads to amyloidosis, which results in various neurodegenerative diseases. Atomic force microscopy (AFM) has proven to be an excellent tool investigating amyloids; it has been extensively utilized to characterize its morphology, assembly process, and mechanical properties. This review summarizes studies which applied AFM to detect the inter- and intramolecular interactions of amyloid fibrils and classified the influencing factors of amyloid’s nanomechanics in detail. The characteristics of amyloid fibrils driven by inter- and intramolecular interactions, including various morphologies of amyloid fibrils, self-assembly process, and the aggregating pathway, are described. Successful examples where AFM provided abundant information about inter- and intramolecular interactions of amyloid fibrils in different environments are presented. Direct force measurement of intra- or intermolecular interactions utilizing an AFM-based tool, single-molecular force spectroscopy (SMFS), is introduced. Some mechanical information such as elasticity, adhesiveness, and strength was obtained by stretching amyloid fibrils. This review helps researchers in understanding the mechanism of amyloidogenesis and exploring the properties of amyloid using AFM techniques.

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