Structure of amyloid fibrils. Medical search. Frequent questions

Amylin, or islet amyloid polypeptide (IAPP), is a 37-residue peptide hormone. (wikipedia.org)
To illustrate the method , we apply it to elucidate the dynamics of an amyloid fibril of the islet amyloid polypeptide (IAPP). (bvsalud.org)
Small molecule inhibitors of islet amyloid polypeptide fibril formation. (jnu.ac.in)
Inhibiting the islet amyloid polypeptide fibril formation by the red wine compound resveratrol. (jnu.ac.in)
The laboratory of Pr Bourgault is studying the mechanisms by which the peptidic hormone islet amyloid polypeptide (IAPP) and the immunoglobulin light chain (LC) protein self-associate to form these well-defined amyloid fibrils. (uqam.ca)
Here, we have characterized the aggregation kinetics, seeding ability, morphology, conformation, stability, and toxicity of amyloid fibrils formed by a 20-residue domain of the islet amyloid polypeptide (IAPP), as well as of a backward and scrambled version of this peptide. (ibecbarcelona.eu)

Studies have shown that fibrils are the end product and not necessarily the most toxic form of amyloid proteins/peptides in general. (wikipedia.org)
Amyloidosis results from the accumulation of pathogenic amyloids-most of which are aggregates of misfolded proteins-in a variety of tissues. (medscape.com)
[ 5 ] Only 10% of amyloidosis deposits consist of components such as glycosaminoglycans (GAGs), apolipoprotein-E (apoE), and serum amyloid P-component (SAP), while nearly 90% of the deposits consist of amyloid fibrils that are formed by the aggregation of misfolded proteins. (medscape.com)
[ 6 ] In humans, about 23 different unrelated proteins are known to form amyloid fibrils in vivo. (medscape.com)
Amyloids, which are proteins notoriously known for their association with neuro-degenerative diseases such as Alzheimer's and Parkinson's, form a network of protein fibrils -- somewhat similar to a spider web -- characterized by an orderly and extremely stable structure. (sciencedaily.com)
The stacked gray arrows are a artistic representations of the amyloid proteins associated with numerous diseases, including Alzheimer's. (uclahealth.org)
When proteins enter amyloid, they stack up like the rungs of a ladder and interfere with normal operations of biological cells. (uclahealth.org)
Prof. Meytal Landau from the Faculty of Biology studies amyloids - fibrillar aggregates of proteins. (technion.ac.il)
As a result, the tetramers break down into individual transthyretin proteins, which attach to each other to form strands called fibrils. (medlineplus.gov)
In this review, we assess the potential role of putative gut microbiota products in the etiopathogeny of Parkinson's disease, with a special emphasis on functional bacterial amyloid proteins, bacterial biosurfactants, endotoxins and short-chain fatty acids. (techscience.com)
Once added to the fibrils, the ends would serve to recruit additional proteins, and the chain lengthens. (virology.ws)
The bacterial chromosomic DNA is packed within a membrane-less structure, the nucleoid, due to the association of DNA with proteins called Nucleoid Associated Proteins (NAPs). (cea.fr)
Many of these proteins bind to metals such as zinc, but the structure of these metal-bound proteins has been difficult to study. (mit.edu)
The specific functional structure of natural proteins is determined by the way in which amino acids are sequentially connected in the polypeptide. (ibecbarcelona.eu)
The tight sequence/structure relationship governing protein folding does not seem to apply to amyloid fibril formation because many proteins without any sequence relationship have been shown to assemble into very similar Î²-sheet-enriched structures. (ibecbarcelona.eu)
The results confirm that, as for globular proteins, highly specific polypeptide sequential traits govern the assembly pathway, final fine structure, and cytotoxic properties of amyloid conformations. (ibecbarcelona.eu)
What distinguishes amyloid ﬁbrils formed by prions from those formed by other proteins is not clear. (pdf-archive.com)
Hence, what diﬀerentiates amyloids formed by bona fide prions from amyloids formed by other proteins is not well understood. (pdf-archive.com)
Recent studies indicate that nanomechanics may play an important role not only in the conversion process of soluble proteins into their ﬁbrillar state, but especially in the key characteristics of prions: their transmissibility.8,9 Amyloid ﬁbrils are highly sensitive to local thermal ﬂuctuations in liquid medium, which cause them to undergo bending along their longitudinal axis. (pdf-archive.com)
We use structure based modeling and computational protein design methods to optimize the protein sequence of proteins and peptides in order to control their assembly. (lu.se)
Misfolding of proteins sometimes leads to the formation of certain type of aggregates, amyloids, which can cause diseases such as Alzheimer's, ParkinsonÕs, type II diabetes and Creutzfeldt-Jakob. (lu.se)
Rebecca Frankel ( Co-assembly of proteins and lipids: From lipodiscs to amyloid aggregates (Co-supervisor. (lu.se)

We demonstrate the effectiveness of this approach by identifying drug-like, head-to-tail cyclic peptides that modulate the aggregation of the Alzheimer's disease-associated amyloid β peptide. (nature.com)
Our results highlight the dual role of short aggregation core motifs in reversible amyloid formation and receptor binding. (nature.com)
A number of non-structural screening attempts have been made to identify natural and synthetic compounds that might prevent the aggregation and toxicity of amyloid fibrils. (uclahealth.org)
Those compounds that showed the strongest potential for binding were then tested for their efficacy in blocking the aggregation of amyloid-beta and for their ability to protect mammalian cells grown in culture from the protein's toxic effects, which in the past has proved very difficult. (uclahealth.org)
Zn(2+) enhances TTR aggregation in vitro, and is a component of ex vivo TTR amyloid fibrils. (rcsb.org)
Partitioning conformational intermediates between competing refolding and aggregation pathways: insights into transthyretin amyloid disease. (medlineplus.gov)
Quantitative analysis of the kinetics of seeded aggregation, using a simple Michaelis-Menten-like model, in which the monomer first binds and then undergoes conformational conversion to β-strand, shows that the fibrils of tau-K18 K280Q convert monomeric protein more slowly than do fibrils of tau-K18. (ncbs.res.in)
First author Anthony Fitzpatrick and colleagues solved the structures by looking at the end product of tau aggregation: the filamentous tangles crowding the cortex of a 74-year-old woman who died after a 10-year history with AD. (alzforum.org)
Polymorphism in the structure of fibrils formed by aggregation suggests the existence of many different assembly pathways and therefore a heterogeneous ensemble of soluble oligomers. (biorxiv.org)
Aggregation to form fibrils is also highly heterogeneous in terms of the number of strands in a fibril and the elongation speed and conformation of fibrils. (biorxiv.org)
This heterogeneity in all stages of aggregation explains diverse and sometimes irreproducible results of experimental studies of amyloid-β. (biorxiv.org)
Its aggregation to form fibrils that are found in brain tissue is one of the key characteristics of Alzheimer's disease. (biorxiv.org)
Although fibrils are known to be toxic, a number of experimental studies also suggest that a subset of soluble oligomers, transiently appearing during the aggregation process, are more responsible for disease pathology than the fibril itself 2 - 6 . (biorxiv.org)
To better understand the pathogenic mechanism, therefore, it is important to characterize the entire aggregation process from the initial oligomerization to the formation and growth of fibrils. (biorxiv.org)
Despite tremendous effort to understand aggregation of Aβ to form oligomers and fibrils, experimental results vary widely and there is no consensus on the model for these processes 7 . (biorxiv.org)
Interestingly, there are variations in the fibril structure 9 , 10 depending on various factors such as aggregation conditions. (biorxiv.org)
In this initial study, we combine single-molecule Förster resonance energy transfer (FRET) spectroscopy, fluorescence lifetime imaging (FLIM), and image analysis using deep learning (codes are available at https://github.com/hoisunglab/FNet ) to interrogate several steps during the aggregation process of the 42-residue Aβ peptide (Aβ42), including dimerization, formation of stable oligomers, and fibril elongation. (biorxiv.org)
Protein aggregation and amyloid deposition are associated with diseases as diverse as Alzheimer's disease, diabetes mellitus type 2 (DM-2), Creutzfel-Jakob disease and numerous amyloidoses. (uqam.ca)
ABSTRACT Self-templated protein aggregation and intracerebral deposi- tion of aggregates, sometimes in the form of amyloid ﬁbrils, is a hallmark of mammalian prion diseases. (pdf-archive.com)
Currently he is working in the area of protein structure, function, protein misfolding / aggregation and amyloid induction and inhibition at Aligarh Muslim University. (eurekaselect.com)
A multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation. (nih.gov)

Nucleation and growth of amyloid fibrils were found to only occur in supersaturated solutions above a critical concentration (ccrit). (researchgate.net)
Nucleation and Growth of Amyloid Fibrils. (acs.org)

The structure of PrP Sc protein has been elusive, because it forms aggregates and amyloid fibrils. (virology.ws)

IAPP is capable of forming amyloid fibrils in vitro. (wikipedia.org)
Determination of the Structure and Dynamics of the Fuzzy Coat of an Amyloid Fibril of IAPP Using Cryo-Electron Microscopy. (bvsalud.org)
NMR spectroscopic investigation of early events in IAPP amyloid fibril formation. (jnu.ac.in)
The three IAPP peptides readily aggregate into ordered, Î²-sheet-enriched, amyloid-like fibrils. (ibecbarcelona.eu)

All types of amyloid consist of one major fibrillar protein that defines the type of amyloid. (medscape.com)
At some point we knew that we had found something unique, but only after several trips to cyclic particle accelerators (Synchrotrons) in Grenoble and Chicago were we successful in verifying its being a new type of amyloid," said Prof. Landau. (sciencedaily.com)
Retention and accumulation of this type of amyloid protein is presumed to be the main pathogenic process underlying beta-2m amyloidosis. (medscape.com)

Neurodegenerative diseases and other amyloidoses are linked to the formation of amyloid fibrils. (nih.gov)
Biochemical, biophysical and biological assays using isolated amyloid β peptide, primary neurons and various established Alzheimer's disease nematode models showed that the selected macrocycles potently inhibit the formation of neurotoxic amyloid β peptide aggregates. (nature.com)
We find that pH sensitivity diminishes in the absence of acidic gatekeepers and amyloid formation progresses over a broad pH range. (nature.com)
Functional amyloids play a beneficial role in a variety of physiologic processes (eg, long-term memory formation, gradual release of stored peptide hormones). (medscape.com)
Such drugs will inhibit the amyloid formation thereby neutralizing one of the important 'weapons' in the arsenal of this pathogenic bacterium. (sciencedaily.com)
Such studies have revealed that polyphenols, naturally occurring compounds found in green tea and in the spice turmeric, can inhibit the formation of amyloid fibrils. (uclahealth.org)
These findings have implications in the study of β-sheet fibril formation, and in the molecular design of materials. (acs.org)
Here, we investigate highly heterogeneous oligomerization and fibril formation of the 42-residue amyloid-β peptide (Aβ42). (biorxiv.org)
In our previous work using single-molecule FRET and MD simulation, we have shown that the monomer of Aβ42 is almost completely disordered with no structured regions that could possibly be a template for fibril formation 11 . (biorxiv.org)
The driving force for the formation of the tight spiral in the twist-bend arrangement is still unclear, and the structure exhibits unusual optical properties that also warrant further study, Zhu said. (lbl.gov)
Due to their central role in disease, significant research efforts are targeted towards interfering with the process of amyloid formation. (lu.se)
Finally, we investigated if the inhibiting effect of DNAJB6 on Aβ fibril formation could be reproduced by an isolated chaperone domain. (lu.se)
We found that the C-terminal domain of DNAJB6 - suggested to be involved in peptide binding after dimerization - will inhibit the secondary nucleation of Aβ fibril formation as opposed to the intact protein which inhibits the primary nucleation. (lu.se)

According to Prof. Landau, "This disease surprised the scientific community because its cause was not a virus, nor a bacterium, but a protein called Prion, possessing an amyloid-like structure. (sciencedaily.com)
The "Mad Cow" prion, like all amyloids discovered so far, belongs to a group possessing what is called a cross-ß structure. (sciencedaily.com)
That's why the newly solved structure of an infectious prion protein is the topic of the sixth prion article at virology blog. (virology.ws)
Clearly solving the structure of prion protein was needed to fully understand the biology of this unusual pathogen. (virology.ws)
The structure of PrP Sc protein provides a mechanism for prion replication by incorporation of additional molecules into a growing beta-solenoid. (virology.ws)
On the basis of previous studies on yeast prions that correlated high intrinsic fragmentation rates of ﬁbrils with prion propagation eﬃciency, it has been hypothesized that the nanomechanical properties of prion amyloid such as strength and elastic modulus may be the distinguishing feature. (pdf-archive.com)
Yeast prions: structure, biology, and prion-handling systems. (nih.gov)
Amyloids and yeast prion biology. (nih.gov)
Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel β-sheet structure. (nih.gov)
Prion diseases of yeast: amyloid structure and biology. (nih.gov)

Amyloid fibrils are protein polymers comprising identical monomer units (homopolymers). (medscape.com)
All four structures reveal three tetra-coordinated Zn(2+)-binding sites (ZBS 1-3) per monomer, plus a fourth site (ZBS 4) involving amino acid residues from a symmetry-related tetramer that is not visible in solution by NMR. (rcsb.org)
We have irradiated amyloid fibrils with a free-electron laser (FEL) tuned to mid-infrared frequencies to induce dissociation of the aggregates into monomer forms. (scirp.org)
It circulates as an unbound monomer distributed in the extracellular space and polymerizes to form amyloid deposits in a variety of tissues. (medscape.com)
Amyloid β peptide: from monomer solubility to fibril structure (Co-supervisor. (lu.se)
Only a small part of the N-terminus of the monomer interacts with the fibril surface of morphology A, compared to a larger part of the monomer for. (lu.se)
Only a small part of the N-terminus of the monomer interacts with the fibril surface of morphology A, compared to a larger part of the monomer for morphology B. Differences in ThT binding seen by fluorescence titrations, and mesoscopic structures seen by cryo-TEM, support the conclusion of the two morphologies having different surface properties. (lu.se)

While these compounds did not reduce the amount of protein aggregates, they were found to reduce the protein's toxicity and to increase the stability of amyloid fibrils - a finding that lends further evidence to the theory that smaller assemblies of amyloid-beta known as oligomers, and not the fibrils themselves, are the toxic agents responsible for Alzheimer's symptoms. (uclahealth.org)
The researchers hypothesize that by binding snugly to the protein, the compounds they identified may be preventing these smaller oligomers from breaking free of the amyloid-beta fibrils, thus keeping toxicity in check. (uclahealth.org)
Although dissociation of amyloid fibril aggregates is expected to lead to a decrease in the toxicity of the fibrils in cells, the fibril structure is robust under physiological conditions. (scirp.org)

Researchers from Amsterdam and Enschede have for the first time performed a structural comparison of two types of amyloid fibrils that have been associated with Parkinson's disease. (uva.nl)

Polymorphisms that slightly vary native peptides or inflammatory processes set the stage for abnormal protein folding and amyloid fibril deposition. (medscape.com)
Amyloidosis is a clinical disorder caused by extracellular and/or intracellular deposition of insoluble abnormal amyloid fibrils that alter the normal function of tissues. (medscape.com)
Amyloidosis is caused by the deposition of amyloid fibrils in various organs of a mammalian body [1] -[3]. (scirp.org)
All recognized mutations for AD are associated with increased deposition of amyloid-beta (Abeta), a peptide fragment comprising 39-43 amino acids that derive from the catabolism of the amyloid precursor protein (APP) molecule. (medscape.com)

The production of toxic Aβ peptides from amyloid precursor protein (APP) proceeds via the sequential cleavage of the extracellular domain by β-secretase, followed by an intramembrane cut by γ-secretase. (alzforum.org)
The muscarinic acetylcholine receptor has been a target for AD therapies for decades, based first on the loss of acetylcholine in the disease and the role of M1 receptors in memory and cognition, and then on the finding that the receptors control the processing of amyloid precursor protein to Aβ peptides. (alzforum.org)
Amyloid-β (Aβ) is a peptide fragment consisting of 39 - 43 amino acid residues, which is produced by successive proteolytic cleavages of the amyloid precursor protein (APP) 1 . (biorxiv.org)

Using a combination of experimental methods they show that a cytotoxic C-terminal truncated form of the alpha-synuclein protein that is abundant in vivo, aggregates into more strongly twisted fibrils that are more exposed to water. (uva.nl)

Native or wild-type quaternary protein structure is usually born from a single translated protein sequence with one ordered conformation with downstream protein interactions. (medscape.com)

The researchers discovered, for the first time, unique amyloid fibrils through which the pathogenic and highly drug resistant Staphylococcus aureus bacterium attacks the human cells and immune system. (sciencedaily.com)

Amyloids are implicated in neurodegenerative diseases. (nih.gov)
Deciphering new structures of amyloids might lead to new insights regarding mechanisms of neurodegenerative diseases. (sciencedaily.com)
Amyloids are associated with numerous human diseases, including microbial and neurodegenerative diseases. (technion.ac.il)
Amyloid fibrillar aggregates isolated from the brains of patients with neurodegenerative diseases invariably have post-translational modifications (PTMs). (ncbs.res.in)
Several neurodegenerative diseases, including Alzheimer's, Parkinson's, or Huntington's disease, are also associated with the presence of amyloid ﬁbrils in the brain of patients. (pdf-archive.com)

While amyloids are often associated with diseases such as Alzheimer's and Parkinson's diseases, other amyloids have normal biological functions. (mit.edu)

By elucidating the key structural aspects of the two fibrillar species, especially of the more cytotoxic 1-108-αS fibrils, the researchers hope to provide clues contributing to an understanding of molecular mechanisms underlying Parkinson's and other related amyloid diseases. (uva.nl)
The resulting conformational ensemble provides an accurate description of the structural variability of the disordered region of the amyloid fibril , known as fuzzy coat. (bvsalud.org)
The conformational ensemble also reveals that in nearly half of the structural core of this amyloid fibril , the side chains exhibit liquid-like dynamics despite the presence of the highly ordered network backbone of hydrogen bonds characteristic of the cross-ß structure of amyloid fibrils . (bvsalud.org)
The Lys 280 ➔ Gln mutation mimicking disease-linked acetylation of Lys 280 in tau extends the structural core of fibrils and modulates their catalytic properties. (ncbs.res.in)
In this study, tau-K18 K280Q, in which the Lys 280 ➔ Gln mutation is used to mimic acetylation at Lys 280, is shown, using HX-MS measurements, to form fibrils with a structural core that is longer than that of tau-K18 fibrils. (ncbs.res.in)
We have previously succeeded in dissociating fibril structures of a short peptide of the thyroid hormone by tuning the oscillation frequency to the amide I band, but the detailed structural changes of the peptide have not yet been determined at a high spatial resolution. (scirp.org)
Synchrotron-radiation infrared microscopy (SR-IRM) is a powerful tool for in situ analysis of minute structural changes of various materials, and in this study, the feasibility of SR-IRM for analyzing the microscopic conformational changes of amyloid fibrils after FEL irradiation was investigated. (scirp.org)
X-ray crystallography and nuclear magnetic resonance (NMR) are usually employed to determine the structure of peptides [15] -[17] , but while these analytical methods are excellent for three-dimensional structural determination at the atomic level, they are also time consuming, and once analyzed, samples cannot be re-used for other analytical methods. (scirp.org)
Even though there has been a lot of high-resolution, atomic level structural work on amyloids by solid-state NMR, people have really not studied the metal-binding aspects," says professor Mei Hong. (mit.edu)
Even though there has been a lot of high-resolution, atomic level structural work on amyloids by solid-state NMR, people have really not studied the metal-binding aspects," says Mei Hong, an MIT professor of chemistry and one of the senior authors of the paper, which appears in the Proceedings of the National Academy of Sciences the week of May 29. (mit.edu)
LRRs are composed of consecutively arranged structural units (repeats) that form elongated structure. (lu.se)

The modern era of amyloidosis classification began in the late 1960s with the development of methods to solubilize amyloid fibrils. (medscape.com)
Most of the TTR gene variants that cause transthyretin amyloidosis alter the structure of transthyretin, impairing its ability to form tetramers. (medlineplus.gov)
The fibrils clump together and form amyloid deposits in certain tissues, leading to the signs and symptoms of transthyretin amyloidosis. (medlineplus.gov)
Amyloid fibrils are widely recognized as a cause of serious amyloidosis such as Alzheimer's disease. (scirp.org)

The triggers for the pathologic amyloid transformation of alpha-synuclein remain unknown. (techscience.com)
alpha-synuclein: amyloid fibrils and interactions with lipid membranes (Co-supervisor. (lu.se)

This result demonstrates that conformational changes of the fibril structure after the FEL irradiation can be observed at a high spatial resolution using SR-IRM analysis and the FEL irradiation system can be useful for dissociation of amyloid aggregates. (scirp.org)
An auto-catalytic surface for conformational replication of amyloid fibrils- Genesis of an amyloid world? (jnu.ac.in)

UCLA chemists and molecular biologists have for the first time used a "structure-based" approach to drug design to identify compounds with the potential to delay or treat Alzheimer's disease, and possibly Parkinson's, Lou Gehrig's disease and other degenerative disorders. (uclahealth.org)

Researchers have discovered unique amyloid fibers used by the highly drug resistant Staphylococcus aureus bacterium (which causes MRSA). (sciencedaily.com)
which bind to amyloid fibers. (uclahealth.org)
Aβ forms amyloid fibrils, long fibers with parallel (or anti-parallel) β-sheet structures (cross-β structure). (biorxiv.org)

The characteristic staggering of the nonplanar subunits results in markedly different fibril ends, termed "groove" and "ridge," leading to different binding pathways on both fibril ends, which has implications for fibril growth. (nih.gov)
The results show different surface properties of the two morphologies, A and B. NMR measurements show that monomers interact differently with the different fibril surfaces. (lu.se)

Fibrillar aggregates of the amyloid-β protein (Aβ) are the main component of the senile plaques found in brains of Alzheimer's disease patients. (nih.gov)

Spectroscopic characterization of diverse amyloid fibrils in-vitro by the fluorescent dye Nile red. (jnu.ac.in)
Recently, it has been shown in vitro that Hfq forms amyloid-like structures through its C-terminal region, hence belonging to the bridging family of NAPs. (cea.fr)

The UCLA researchers, led by David Eisenberg, director of the UCLA-Department of Energy Institute of Genomics and Proteomics and a Howard Hughes Medical Institute investigator, report the first application of this technique in the search for molecular compounds that bind to and inhibit the activity of the amyloid-beta protein responsible for forming dangerous plaques in the brain of patients with Alzheimer's and other degenerative diseases. (uclahealth.org)

Amyloids are clumps of protein fragments that stick together to form stringy fibrils such as the plaques seen in the brains of Alzheimer's patients. (mit.edu)
An amyloid fibrillar form of these peptides is the major component of amyloid plaques found in individuals with Alzheimer's disease and in aged individuals with trisomy 21 (DOWN SYNDROME). (bvsalud.org)

We present the structure of an Aβ(1-42) fibril composed of two intertwined protofilaments determined by cryo-electron microscopy (cryo-EM) to 4.0-angstrom resolution, complemented by solid-state nuclear magnetic resonance experiments. (nih.gov)
In recent years, major advances in cryo-electron microscopy (cryo-EM) have enabled the routine determination of complex biomolecular structures at atomistic resolution. (bvsalud.org)
The structure of PrP Sc protein has now been solved by cryo-electron microscopy and image reconstruction ( link to paper ). (virology.ws)

Common to all forms of prions is the ability to form highly ordered protein aggregates, so-called amyloid ﬁbrils. (pdf-archive.com)

It has been shown that the ability to form these fibrils is coded by the amino acid sequence. (nih.gov)
The researchers discovered 'ammunition' that assists the infectious bacterium: a novel form of an amyloid fibril whose three-dimensional structure was determined at atomic resolution, revealing the first-of-its-kind structure of this toxic fibril. (sciencedaily.com)
All of these diseases are marked by harmful, elongated, rope-like structures known as amyloid fibrils, linked protein molecules that form in the brains of patients. (uclahealth.org)
The structure of this form of the PrP Sc protein reveals that it consists of two intertwined fibrils (red in the image) which most likely consist of a series of repeated beta-strands, or rungs, called a beta-solenoid . (virology.ws)
Two of these Cs tethered together to form each rung of the fibril. (alzforum.org)
Two C-shaped structures, each formed by a molecule of tau, bound together to form individual rungs along the filament. (alzforum.org)
To determine if the R3 and R4 domains were necessary and sufficient to form the core, they treated their filament samples with pronase, which is known to remove all but the cores of tau fibrils. (alzforum.org)
The findings could also help explain how so-called "chiral" structure-molecules can exhibit wildly different properties based on their left- or right-handedness (chirality), which is of interest in biology, materials science and chemistry-can form from organic molecules that do not exhibit such handedness. (lbl.gov)
In the twist-bend phase, the spiraling structure they form resembles a bunch of snakes lined up and then wound snugly around the length of an invisible pole. (lbl.gov)
Researchers at UCSF and Syracuse designed the amyloid protein to catalyze a specific reaction: combining carbon dioxide and water to form bicarbonate. (mit.edu)
Using NMR, the researchers first determined that the peptides form a long fibril chain that consists of layers of structures called beta sheets. (mit.edu)
Here, we show that two chemically identical but morphologically distinct α-synuclein fibrils can form under identical conditions. (lu.se)

Armed with a precise knowledge of the atomic structure of the amyloid-beta protein, Jiang, Eisenberg and colleagues conducted a computational screening of 18,000 compounds in search of those most likely to bind tightly and effectively to the protein. (uclahealth.org)
Computational modeling of the relationship between amyloid and disease. (nih.gov)

A large group of hormones are stored as amyloid fibrils in acidic secretion vesicles before they are released into the bloodstream and readopt their functional state. (nature.com)
An increasing number of physiological roles have been revealed and associated with functional amyloids 1 . (nature.com)
Yeast Prions Compared to Functional Prions and Amyloids. (nih.gov)

2023). Cryo-EM structure of the full-length hnRNPA1 amyloid fibril. (upenn.edu)

Later amyloid fiber structures also seem to have some cytotoxic effect on cell cultures. (wikipedia.org)

Knowledge regarding amyloid fibril structure and the mechanism behind it has been elucidated through the development of protocols rendering reproducible kinetic data in buffer systems. (lu.se)

In the study to be funded by the ERC grant, Prof. Landau will delve into amyloid structure-function relationships and mechanisms, hoping to gain insights for rational design of antimicrobials. (technion.ac.il)
Binding Mechanisms of Amyloid-like Peptides to Lipid Bilayers and Effects of Divalent Cations. (acs.org)

Within the fibrillization reaction, the early prefibrillar structures are extremely toxic to beta-cell and insuloma cell cultures. (wikipedia.org)

These structures suggest that the enhanced amyloidogenicity of the modified Aβ segments may also reduce the concentration required to achieve nucleation and therefore help spur the pathogenesis of AD. (rcsb.org)

2022. Editorial: Advances in Molecular Docking and Structure-Based Modelling. . (ncbs.res.in)

Methylene blue inhibits amyloid Aβ oligomerization by promoting fibrillization. (nature.com)
Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade. (medscape.com)

We probed the effects of biliverdin (BV) binding and its complex with Zn 2+ ions on the structure and HP stability of apoMb. (cea.fr)
We are probing the relation between the supramolecular organization, the molecular architecture and the stability to develop amyloids with precise dynamic properties. (uqam.ca)
The same reasons that make amyloids lethal in biology make them useful as biomaterials (such as their superior stability). (lu.se)

[ 2 ] Many classic eponymic diseases were later found to be related to a diverse array of misfolded polypeptides (amyloid) that contain the common beta-pleated sheet architecture. (medscape.com)
Structure-based drug design, in which the physical structure of a targeted protein is used to help identify compounds that will interact with it, has already been used to generate therapeutic agents for a number of infectious and metabolic diseases. (uclahealth.org)

Hydrogen-deuterium exchange mapping of Abeta 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy. (jnu.ac.in)

Various descriptive classification systems were proposed based on the organ distribution of amyloid deposits and clinical findings. (medscape.com)
In addition, microglia phagocytoses brain-specific cargo, such as axonal and myelin debris in spinal cord injury or multiple sclerosis, amyloid-β deposits in Alzheimer's disease, and supernumerary synapses in postnatal development. (frontiersin.org)
The most severe complication involves beta-2m amyloid deposits destroying paravertebral ligaments and intervertebral discs, which can result in paraplegia. (medscape.com)

The amyloid fibrils are well-organized nanostructures that results from the self-assembly of a given polypeptide chain. (uqam.ca)

See also: Formulation of amyloid fibrils susceptible to salt concentration. (uva.nl)

Proislet amyloid polypeptide (proIAPP, proamylin, proislet protein) is produced in the pancreatic beta cells (β-cells) as a 67 amino acid, 7404 Dalton pro-peptide and undergoes post-translational modifications including protease cleavage to produce amylin. (wikipedia.org)
We report the observation of intermediate structures in the self-assembly of the peptide KFE8 (FKFEFKFE), designed with alternating polar and nonpolar amino acids. (acs.org)
The 3.4Å resolution allowed the researchers to discern the amino acids incorporated into the fibril core. (alzforum.org)
Each C-shaped structure spanned amino acids V 306 -F 378 , which contained the entire R3 and R4 repeat domains, plus an additional 10 amino acids C-terminal to the repeats. (alzforum.org)

The researchers do not report whether cognition was negatively affected in the animals, either by M1 loss or enhanced amyloid accumulation. (alzforum.org)

Accordingly, the group of Pr Bourgault , in collaboration with Pr Marcotte and Pr Rouiller , is evaluating the usage of amyloid fibrils as a novel formulation/delivery approach for peptide therapeutics. (uqam.ca)

Although the secondary structure of host-encoded cellular PrP (PrP C ) is predominantly α-helical, during disease its relatively underglycosylated infectious counterpart (PrP Sc ) assembles into amyloid fibrils with parallel, in-register, intermolecular β-sheets ( 1 - 7 ). (cdc.gov)

Atomic Insights into Amyloid-Induced Membrane Damage. (acs.org)

Fibrils of morphology B were found to have lower solubility than A. This indicates that fibrils of morphology B are thermodynamically more stable, implying a chemical potential of fibrils of morphology B that is lower than that of morphology A. Consequently, at prolonged incubation time, fibrils of morphology B remained B, while an initially monomorphic sample of morphology A gradually transformed to B. (lu.se)

The roles that PTMs play in modulating the structures and polymorphism of amyloid aggregates, and hence their ability to catalyze the conversion of monomeric protein to their fibrillar structure is, however, poorly understood. (ncbs.res.in)

The atomic interactions between subunits in protein assemblies are finely tuned to control affinity as well as quaternary structure. (lu.se)

Powder diffraction patterns suggest a similar structure may be adopted by protofilaments of an analogous segment containing the heritable Iowa mutation, Asp23Asn. (rcsb.org)

The molecular biology and clinical features of amyloid neuropathy. (medlineplus.gov)
Crafting a technique that has become his claim to fame, Sjors Scheres of the MRC Laboratory of Molecular Biology in Cambridge, England, teamed up with Michel Goedert, also at MRC, to solve 3.4-Angstrom resolution structures of both straight and paired helical filaments of tau. (alzforum.org)

It makes up the beta chain of the human leukocyte antigen (HLA) class I molecule and has the prominent beta-pleated structure that is characteristic of amyloid fibrils. (medscape.com)
The measurements show that the liquid crystals complete a 360-degree twist-bend over a distance of just 8 nanometers at room temperature, which Zhu said is an "amazingly short" distance given that each molecule is 3 nanometers long, and such a strongly coiled structure is very rare. (lbl.gov)

The distance between the hydrogen-bonded protein sheets within the fibril appears to be greater. (uva.nl)

MHC macromolecular structure. (medscape.com)

The researchers conclude that fibrils formed by 1-108-αS are more-strongly twisted and that - perhaps due to the stronger twist - their fibril core is more exposed to water. (uva.nl)
Researchers examined the spiral "twist-bend" structure (right) formed by boomerang-shaped liquid crystal molecules (left and center) measuring 3 nanometers in length, using a pioneering X-ray technique at Berkeley Lab's Advanced Light Source. (lbl.gov)
A team of MIT chemists, working with researchers at the University of California at San Francisco (UCSF) and Syracuse University, has now deciphered the structure of an amyloid that binds to zinc. (mit.edu)
The UCSF and Syracuse researchers first reported their artificial amyloid in 2014. (mit.edu)

Anatomy16

Organisms7

Diseases16

Chemicals and Drugs83

Analytical, Diagnostic and Therapeutic Techniques and Equipment39

Psychiatry and Psychology1

Phenomena and Processes38

Disciplines and Occupations3

Technology, Industry, Agriculture2

Information Science4

Health Care1

Islet amyloid pol6

Proteins22

Aggregation21

Growth of amyloid fibrils2

Aggregates and amyloid fibrils1

IAPP4

Type of amyloid3

FORMATION13

Prion10

Monomer7

Toxicity3

Types of amyloid1

Deposition4

Precursor3

Vivo1

Conformation1

Pathogenic1

Neurodegenerative diseases5

Alzheimer's and Parkinson's1

Structural11

Amyloidosis4

Alpha-synuclein2

Conformational2

Parkinson's1

Fibers3

Different fibril2

Fibrillar aggregates1

Vitro2

Inhibit1

Plaques2

Cryo-electron m3

Protein aggregates1

Form12

Computational2

Functional3

20231

Cytotoxic1

Mechanism1

Mechanisms2

Toxic1

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20221

Inhibits2

Stability3

Diseases2

Abeta1

Deposits3

Nanostructures1

Concentration1

Amino4

Accumulation1

Formulation1

Infectious1

Insights1

Solubility1

Polymorphism1

Atomic1

Diffraction1

Biology2

Molecule2

Hydrogen1

Macromolecular structure1

Researchers4