scholarly journals “What Doesn’t Kill You Makes You Stronger”: Future Applications of Amyloid Aggregates in Biomedicine

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5245
Author(s):  
Sherin Abdelrahman ◽  
Mawadda Alghrably ◽  
Joanna Izabela Lachowicz ◽  
Abdul-Hamid Emwas ◽  
Charlotte A. E. Hauser ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Biomedical Applications ◽  
Amyloid Aggregation ◽  
Factors Affecting ◽  
Amyloid Peptides ◽  
Amyloid Aggregates ◽  
Innovative Materials ◽  
Functional Amyloids ◽  
Innovative Medicine ◽  
Aggregation Factors

Amyloid proteins are linked to the pathogenesis of several diseases including Alzheimer’s disease, but at the same time a range of functional amyloids are physiologically important in humans. Although the disease pathogenies have been associated with protein aggregation, the mechanisms and factors that lead to protein aggregation are not completely understood. Paradoxically, unique characteristics of amyloids provide new opportunities for engineering innovative materials with biomedical applications. In this review, we discuss not only outstanding advances in biomedical applications of amyloid peptides, but also the mechanism of amyloid aggregation, factors affecting the process, and core sequences driving the aggregation. We aim with this review to provide a useful manual for those who engineer amyloids for innovative medicine solutions.

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 Evolutionary Conservation of Systemic and Reversible Amyloid Aggregation

2021 ◽  
Author(s):  
Emma Lacroix ◽  
Lionel Pereira ◽  
Byoungjoo Yoo ◽  
Krysta M. Coyle ◽  
Sahil Chandhok ◽  
...  
Keyword(s):  
Protein Conformation ◽  
Low Complexity ◽  
Evolutionary Conservation ◽  
Amyloid Aggregation ◽  
Diverse Species ◽  
Amyloid Aggregates ◽  
Stress Response Pathway ◽  
Evolutionarily Conserved ◽  
Non Coding Rnas ◽  
Functional Amyloids

In response to environmental stress, human cells have been shown to form reversible amyloid aggregates within the nucleus, termed amyloid bodies (A-bodies). These protective physiological structures share many of the biophysical characteristics associated with the pathological amyloids found in Alzheimer's and Parkinson's disease. Here, we show that A-bodies are evolutionarily conserved across the eukaryotic domain, with their detection in D. melanogaster and S. cerevisiae marking the first examples of these functional amyloids being induced outside of a cultured cell setting. The conditions triggering amyloidogenesis varied significantly among the species tested, with results indicating that A-body formation is a severe, but sub-lethal, stress response pathway that is tailored to an organism's environmental norms. RNA-sequencing analyses demonstrate that the regulatory low-complexity long non-coding RNAs that drive A-body aggregation are both conserved and essential in human, mouse, and chicken cells. Thus, the identification of these natural and reversible functional amyloids in a variety of evolutionarily diverse species, highlights the physiological significance of this protein conformation and will be informative in advancing our understanding of both functional and pathological amyloid aggregation events.

Role of the Structural Characteristics of Dendrimers in the Manifestation of the Antiamyloid Properties

INEOS OPEN ◽  
2020 ◽  
Vol 3 ◽  
Author(s):  
S. A. Sorokina ◽  
◽  
Yu. Yu. Stroilova ◽  
V. I. Muronets ◽  
Z. B. Shifrina ◽  
...  
Keyword(s):  
Neurodegenerative Diseases ◽  
Structural Characteristics ◽  
Short Review ◽  
External Factors ◽  
Amyloid Aggregation ◽  
Amyloid Proteins ◽  
Molecular Parameters ◽  
Amyloid Aggregates ◽  
Aggregation Processes

Among the compounds able to efficiently inhibit the amyloid aggregation of proteins and decompose the amyloid aggregates that cause neurodegenerative diseases, of particular interest are dendrimers, which represent individual macromolecules with the hypercrosslinked architectures and given molecular parameters. This short review outlines the peculiarities of the antiamyloid activity of dendrimers and discusses the effect of dendrimer structures and external factors on their antiamyloid properties. The potential of application of dendrimers in further investigations on the aggregation processes of amyloid proteins as the compounds that exhibit the remarkable antiamyloid activity is evaluated.

scholarly journals Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein

Molecules ◽  
2021 ◽  
Vol 26 (8) ◽  
pp. 2371
Author(s):  
Valeria Guarrasi ◽  
Giacoma Cinzia Rappa ◽  
Maria Assunta Costa ◽  
Fabio Librizzi ◽  
Marco Raimondo ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Environmental Sustainability ◽  
Bovine Milk ◽  
Amyloid Formation ◽  
Aggregation Process ◽  
Amyloid Aggregation ◽  
Social Challenges ◽  
Force Microscopy ◽  
Atomic Force ◽  
Apple Peels

Waste valorization represents one of the main social challenges when promoting a circular economy and environmental sustainability. Here, we evaluated the effect of the polyphenols extracted from apple peels, normally disposed of as waste, on the amyloid aggregation process of κ-casein from bovine milk, a well-used amyloidogenic model system. The effect of the apple peel extract on protein aggregation was examined using a thioflavin T fluorescence assay, Congo red binding assay, circular dichroism, light scattering, and atomic force microscopy. We found that the phenolic extract from the peel of apples of the cultivar “Fuji”, cultivated in Sicily (Caltavuturo, Italy), inhibited κ-casein fibril formation in a dose-dependent way. In particular, we found that the extract significantly reduced the protein aggregation rate and inhibited the secondary structure reorganization that accompanies κ-casein amyloid formation. Protein-aggregated species resulting from the incubation of κ-casein in the presence of polyphenols under amyloid aggregation conditions were reduced in number and different in morphology.

scholarly journals Promiscuous Cross-seeding between Bacterial Amyloids Promotes Interspecies Biofilms

2012 ◽  
Vol 287 (42) ◽  
pp. 35092-35103 ◽  
Author(s):  
Yizhou Zhou ◽  
Daniel Smith ◽  
Bryan J. Leong ◽  
Kristoffer Brännström ◽  
Fredrik Almqvist ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Shewanella Oneidensis ◽  
Bacterial Attachment ◽  
Surface Attachment ◽  
E Coli ◽  
Amyloid Aggregates ◽  
Functional Amyloids ◽  
Biofilm Development ◽  
Distant Homolog

Amyloids are highly aggregated proteinaceous fibers historically associated with neurodegenerative conditions including Alzheimers, Parkinsons, and prion-based encephalopathies. Polymerization of amyloidogenic proteins into ordered fibers can be accelerated by preformed amyloid aggregates derived from the same protein in a process called seeding. Seeding of disease-associated amyloids and prions is highly specific and cross-seeding is usually limited or prevented. Here we describe the first study on the cross-seeding potential of bacterial functional amyloids. Curli are produced on the surface of many Gram-negative bacteria where they facilitate surface attachment and biofilm development. Curli fibers are composed of the major subunit CsgA and the nucleator CsgB, which templates CsgA into fibers. Our results showed that curli subunit homologs from Escherichia coli, Salmonella typhimurium LT2, and Citrobacter koseri were able to cross-seed in vitro. The polymerization of Escherichia coli CsgA was also accelerated by fibers derived from a distant homolog in Shewanella oneidensis that shares less than 30% identity in primary sequence. Cross-seeding of curli proteins was also observed in mixed colony biofilms with E. coli and S. typhimurium. CsgA was secreted from E. coli csgB− mutants assembled into fibers on adjacent S. typhimurium that presented CsgB on its surfaces. Similarly, CsgA was secreted by S. typhimurium csgB− mutants formed curli on CsgB-presenting E. coli. This interspecies curli assembly enhanced bacterial attachment to agar surfaces and supported pellicle biofilm formation. Collectively, this work suggests that the seeding specificity among curli homologs is relaxed and that heterogeneous curli fibers can facilitate multispecies biofilm development.

Photopolymerized PVA-g-GMA Hydrogels for Biomedical Applications: Factors Affecting Hydrogel Formation and Bioevaluation Tests

2018 ◽  
Vol 43 (7) ◽  
pp. 3565-3575 ◽  
Author(s):  
Elbadawy A. Kamoun ◽  
Ahmed M. Omer ◽  
Marwa M. Abu-Serie ◽  
Sherine N. Khattab ◽  
Heba M. Ahmed ◽  
...  
Keyword(s):  
Biomedical Applications ◽  
Factors Affecting ◽  
Hydrogel Formation

scholarly journals Stability of Engineered Micro or Nanobubbles for Biomedical Applications

Pharmaceutics ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 1089
Author(s):  
Beomjin Park ◽  
Semi Yoon ◽  
Yonghyun Choi ◽  
Jaehee Jang ◽  
Soomin Park ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Biomedical Applications ◽  
Ultrasonic Field ◽  
Nanometer Scale ◽  
Factors Affecting ◽  
The Core ◽  
Bubble Structure ◽  
The Stability ◽  
The Relationship

A micro/nanobubble (MNB) refers to a bubble structure sized in a micrometer or nanometer scale, in which the core is separated from the external environment and is normally made of gas. Recently, it has been confirmed that MNBs can be widely used in angiography, drug delivery, and treatment. Thus, MNBs are attracting attention as they are capable of constructing a new contrast agent or drug delivery system. Additionally, in order to effectively use an MNB, the method of securing its stability is also being studied. This review highlights the factors affecting the stability of an MNB and the stability of the MNB within the ultrasonic field. It also discusses the relationship between the stability of the bubble and its applicability in vivo.

Effects ofin vivoconditions on amyloid aggregation

2019 ◽  
Vol 48 (14) ◽  
pp. 3946-3996 ◽  
Author(s):  
Michael C. Owen ◽  
David Gnutt ◽  
Mimi Gao ◽  
Sebastian K. T. S. Wärmländer ◽  
Jüri Jarvet ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibrils ◽  
Amyloid Aggregation ◽  
Comprehensive Overview ◽  
Grand Challenges ◽  
Biophysical Chemistry

One of the grand challenges of biophysical chemistry is to understand the principles that govern protein aggregation leading to amyloid fibrils, which is a highly complex and sensitive process. This review provides a comprehensive overview of how amyloid aggregation is affected by the variousin vivoconstituents and conditions.

scholarly journals A 3D-Printed Multi-Chamber Device Allows Culturing Cells On Buckypapers Coated With PAMAM Dendrimer And Obtain Innovative Materials For Biomedical Applications

2019 ◽  
Vol Volume 14 ◽  
pp. 9295-9306 ◽  
Author(s):  
Alessandro Paolini ◽  
Giulia Battafarano ◽  
Valentina D'Oria ◽  
Francesco Mura ◽  
Simona Sennato ◽  
...  
Keyword(s):  
Biomedical Applications ◽  
Pamam Dendrimer ◽  
Innovative Materials ◽  
3D Printed

scholarly journals Catechins as Tools to Understand the Molecular Basis of Neurodegeneration

Molecules ◽  
2020 ◽  
Vol 25 (16) ◽  
pp. 3571
Author(s):  
Karla Martinez Pomier ◽  
Rashik Ahmed ◽  
Giuseppe Melacini
Keyword(s):  
Phenolic Compounds ◽  
Neurodegenerative Disorders ◽  
Molecular Basis ◽  
Protein Misfolding ◽  
Molecular Mechanisms ◽  
Amyloid Aggregation ◽  
Amyloid Aggregates ◽  
Parkinson’S Diseases ◽  
Pharmacokinetic Properties ◽  
Self Association

Protein misfolding as well as the subsequent self-association and deposition of amyloid aggregates is implicated in the progression of several neurodegenerative disorders including Alzheimer’s and Parkinson’s diseases. Modulators of amyloidogenic aggregation serve as essential tools to dissect the underlying molecular mechanisms and may offer insight on potential therapeutic solutions. These modulators include green tea catechins, which are potent inhibitors of amyloid aggregation. Although catechins often exhibit poor pharmacokinetic properties and bioavailability, they are still essential tools for identifying the drivers of amyloid aggregation and for developing other aggregation modulators through structural mimicry. As an illustration of such strategies, here we review how catechins have been used to map the toxic surfaces of oligomeric amyloid-like species and develop catechin-based phenolic compounds with enhanced anti-amyloid activity.

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