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Journal articles on the topic 'Β-amyloid structures'

Author: Grafiati

Published: 23 November 2024

Last updated: 31 July 2025

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1

Taguchi, Yuzuru, Hiroki Otaki та Noriyuki Nishida. "Mechanisms of Strain Diversity of Disease-Associated in-Register Parallel β-Sheet Amyloids and Implications About Prion Strains". Viruses 11, № 2 (2019): 110. http://dx.doi.org/10.3390/v11020110.

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The mechanism of prion strain diversity remains unsolved. Investigation of inheritance and diversification of protein-based pathogenic information demands the identification of the detailed structures of abnormal isoforms of the prion protein (PrPSc); however, achieving purification is difficult without affecting infectivity. Similar prion-like properties are recognized also in other disease-associated in-register parallel β-sheet amyloids including Tau and α-synuclein (αSyn) amyloids. Investigations into structures of those amyloids via solid-state nuclear magnetic resonance spectroscopy and

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2

M Smith, Margaret, and James Melrose. "Amyloid, A Jekyll and Hyde Molecule, Induces Neuronal Decline and Cognitive Dysfunction but is also a Unique Molecular Template used in Nano-Electronics, Light Capture Photovoltaics, Biosensors and in Neuromorphic Computing." International Journal of Nanotechnology and Nanomedicine 9, no. 2 (2024): 01–13. http://dx.doi.org/10.33140/ijnn.09.02.02.

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This study, examined the self-assembly of amyloid peptides β-40 or β-42 to form neurotoxic plaque and neurofibrillary tangles, neuronal dysfunction and diseases of cognitive decline (e.g. Alzheimer’s, Parkinson’s and Huntington's disease). However, not all amyloids are toxic, functional amyloids are non-toxic ordered structures that have been used in tissue engineering applications. Long and hollow amyloid fibres and flattened tube and spiral ribbon-like structures are diverse self-assembling structures that have found application in the development of next generation computers and biosensors,

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3

Chatani, Eri, Keisuke Yuzu, Yumiko Ohhashi, and Yuji Goto. "Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils." International Journal of Molecular Sciences 22, no. 9 (2021): 4349. http://dx.doi.org/10.3390/ijms22094349.

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Amyloid fibrils are supramolecular protein assemblies represented by a cross-β structure and fibrous morphology, whose structural architecture has been previously investigated. While amyloid fibrils are basically a main-chain-dominated structure consisting of a backbone of hydrogen bonds, side-chain interactions also play an important role in determining their detailed structures and physicochemical properties. In amyloid fibrils comprising short peptide segments, a steric zipper where a pair of β-sheets with side chains interdigitate tightly is found as a fundamental motif. In amyloid fibrils

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4

Paulus, Agnes, Anders Engdahl, Yiyi Yang, et al. "Amyloid Structural Changes Studied by Infrared Microspectroscopy in Bigenic Cellular Models of Alzheimer’s Disease." International Journal of Molecular Sciences 22, no. 7 (2021): 3430. http://dx.doi.org/10.3390/ijms22073430.

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Alzheimer’s disease affects millions of lives worldwide. This terminal disease is characterized by the formation of amyloid aggregates, so-called amyloid oligomers. These oligomers are composed of β-sheet structures, which are believed to be neurotoxic. However, the actual secondary structure that contributes most to neurotoxicity remains unknown. This lack of knowledge is due to the challenging nature of characterizing the secondary structure of amyloids in cells. To overcome this and investigate the molecular changes in proteins directly in cells, we used synchrotron-based infrared microspec

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Sulatskaya, Anna I., Anastasiia O. Kosolapova, Alexander G. Bobylev та ін. "β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis". International Journal of Molecular Sciences 22, № 21 (2021): 11316. http://dx.doi.org/10.3390/ijms222111316.

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Insoluble protein aggregates with fibrillar morphology called amyloids and β-barrel proteins both share a β-sheet-rich structure. Correctly folded β-barrel proteins can not only function in monomeric (dimeric) form, but also tend to interact with one another—followed, in several cases, by formation of higher order oligomers or even aggregates. In recent years, findings proving that β-barrel proteins can adopt cross-β amyloid folds have emerged. Different β-barrel proteins were shown to form amyloid fibrils in vitro. The formation of functional amyloids in vivo by β-barrel proteins for which th

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6

Gao, Yang, Sophia Schedin-Weiss та Lars O. Tjernberg. "A closer look at pathogenic amyloid-β in Alzheimer’s disease using cryo-electron microscopy: a narrative review". Advanced Technology in Neuroscience 1, № 2 (2024): 177–87. http://dx.doi.org/10.4103/atn.atn-d-24-00014.

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Alzheimer’s disease is a progressive neurodegenerative disorder that affects millions of people worldwide. The identification of amyloid-β in Alzheimer’s disease brains, together with the association of mutations in the amyloid-β precursor protein with Alzheimer’s disease pathology, is the basis of the amyloid cascade hypothesis, which suggests that amyloid-β plays a central role in Alzheimer’s disease pathogenesis. Recent studies have further highlighted the role of intraneuronal amyloid-β in Alzheimer’s disease development. Moreover, the success of anti-amyloid-β immunotherapies supports the

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Alperstein, Ariel M., Joshua S. Ostrander, Tianqi O. Zhang, and Martin T. Zanni. "Amyloid found in human cataracts with two-dimensional infrared spectroscopy." Proceedings of the National Academy of Sciences 116, no. 14 (2019): 6602–7. http://dx.doi.org/10.1073/pnas.1821534116.

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UV light and other factors damage crystallin proteins in the eye lens, resulting in cataracts that scatter light and affect vision. Little information exists about protein structures within these disease-causing aggregates. We examined postmortem lens tissue from individuals with and without cataracts using 2D infrared (2DIR) spectroscopy. Amyloid β-sheet secondary structure was detected in cataract lenses along with denatured structures. No amyloid structures were found in lenses from juveniles, but mature lenses with no cataract diagnosis also contained amyloid, indicating that amyloid struc

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8

Freitas, Raul O., Adrian Cernescu, Anders Engdahl, et al. "Nano-Infrared Imaging of Primary Neurons." Cells 10, no. 10 (2021): 2559. http://dx.doi.org/10.3390/cells10102559.

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Alzheimer’s disease (AD) accounts for about 70% of neurodegenerative diseases and is a cause of cognitive decline and death for one-third of seniors. AD is currently underdiagnosed, and it cannot be effectively prevented. Aggregation of amyloid-β (Aβ) proteins has been linked to the development of AD, and it has been established that, under pathological conditions, Aβ proteins undergo structural changes to form β-sheet structures that are considered neurotoxic. Numerous intensive in vitro studies have provided detailed information about amyloid polymorphs; however, little is known on how amylo

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9

Tycko, Robert. "Molecular structure of amyloid fibrils: insights from solid-state NMR." Quarterly Reviews of Biophysics 39, no. 1 (2006): 1–55. http://dx.doi.org/10.1017/s0033583506004173.

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1. Introduction 22. Sources of structural information in solid-state NMR data 52.1 General remarks 52.2 Chemical shifts, linewidths, and magic-angle spinning 62.3 Dipole–dipole couplings and dipolar recoupling 82.4 Tensor correlation techniques 122.5 Solid-state NMR of aligned samples 142.6 Indirect sources of structural information 152.7 Sample preparation for solid-state NMR 153. Levels of structure in amyloid fibrils 184. Molecular structure of β-amyloid fibrils 254.1 Self-propagating, molecular-level polymorphism in Aβ1–40 fibrils 254.2 Structural model for Aβ1-40 fibrils 284.3 Staggering

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10

Yakupova, Elmira I., Liya G. Bobyleva, Sergey A. Shumeyko, Ivan M. Vikhlyantsev, and Alexander G. Bobylev. "Amyloids: The History of Toxicity and Functionality." Biology 10, no. 5 (2021): 394. http://dx.doi.org/10.3390/biology10050394.

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Proteins can perform their specific function due to their molecular structure. Partial or complete unfolding of the polypeptide chain may lead to the misfolding and aggregation of proteins in turn, resulting in the formation of different structures such as amyloid aggregates. Amyloids are rigid protein aggregates with the cross-β structure, resistant to most solvents and proteases. Because of their resistance to proteolysis, amyloid aggregates formed in the organism accumulate in tissues, promoting the development of various diseases called amyloidosis, for instance Alzheimer’s diseases (AD).

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11

Yu, Xiang, та Jie Zheng. "Polymorphic Structures of Alzheimer's β-Amyloid Globulomers". PLoS ONE 6, № 6 (2011): e20575. http://dx.doi.org/10.1371/journal.pone.0020575.

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12

Flynn, Jessica D., and Jennifer C. Lee. "Raman fingerprints of amyloid structures." Chemical Communications 54, no. 51 (2018): 6983–86. http://dx.doi.org/10.1039/c8cc03217c.

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13

Makshakova, Olga N., Liliya R. Bogdanova, Dzhigangir A. Faizullin, Elena A. Ermakova, and Yuriy F. Zuev. "Sulfated Polysaccharides as a Fighter with Protein Non-Physiological Aggregation: The Role of Polysaccharide Flexibility and Charge Density." International Journal of Molecular Sciences 24, no. 22 (2023): 16223. http://dx.doi.org/10.3390/ijms242216223.

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Proteins can lose native functionality due to non-physiological aggregation. In this work, we have shown the power of sulfated polysaccharides as a natural assistant to restore damaged protein structures. Protein aggregates enriched by cross-β structures are a characteristic of amyloid fibrils related to different health disorders. Our recent studies demonstrated that model fibrils of hen egg white lysozyme (HEWL) can be disaggregated and renatured by some negatively charged polysaccharides. In the current work, using the same model protein system and FTIR spectroscopy, we studied the role of

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14

M Smith, Margaret, та James Melrose. "Advanced Innovative Amyloid Fibril Nanotechnological Applications: β-Sheet Proteins, Protein Aggregation, Cognitive Decline, Microbiome Regulated Tau Protein Release, Photo-Pharmacological Drug Regulation and Development of High Performance Surgical Adhesives". International Journal of Nanotechnology and Nanomedicine 9, № 2 (2024): 01–13. http://dx.doi.org/10.33140/ijnn.09.02.01.

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Amyloid self-assembled from amyloid peptides β-40 or β-42 is notorious due to the neurotoxic effects of β- oligomers in plaque and neurofibrillary tangles, neuronal dysfunction and diseases of cognitive decline such as Alzheimer’s, or Parkinson’s disease. This contrasts with so-called functional amyloids which are non-toxic ordered β-sheet molecular templates amenable to applications in tissue engineering. Long and hollow amyloid fibres, flattened tube and spiral ribbons have been used in engineering applications. Protein β-sheet core structures display diverse biological functionalities explo

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15

Hewetson, Aveline, Nazmul H. Khan, Matthew J. Dominguez, et al. "Maturation of the functional mouse CRES amyloid from globular form." Proceedings of the National Academy of Sciences 117, no. 28 (2020): 16363–72. http://dx.doi.org/10.1073/pnas.2006887117.

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The epididymal lumen contains a complex cystatin-rich nonpathological amyloid matrix with putative roles in sperm maturation and sperm protection. Given our growing understanding for the biological function of this and other functional amyloids, the problem still remains: how functional amyloids assemble including their initial transition to early oligomeric forms. To examine this, we developed a protocol for the purification of nondenatured mouse CRES, a component of the epididymal amyloid matrix, allowing us to examine its assembly to amyloid under conditions that may mimic those in vivo. He

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Balobanov, Vitalii, Rita Chertkova, Anna Egorova, Dmitry Dolgikh, Valentina Bychkova, and Mikhail Kirpichnikov. "The Kinetics of Amyloid Fibril Formation by de Novo Protein Albebetin and Its Mutant Variants." Biomolecules 10, no. 2 (2020): 241. http://dx.doi.org/10.3390/biom10020241.

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Engineering of amyloid structures is one of the new perspective areas of protein engineering. Studying the process of amyloid formation can help find ways to manage it in the interests of medicine and biotechnology. One of the promising candidates for the structural basis of artificial functional amyloid fibrils is albebetin (ABB), an artificial protein engineered under the leadership of O.B. Ptitsyn. Various aspects of the amyloid formation of this protein and some methods for controlling this process are investigated in this paper. Four stages of amyloid fibrils formation by this protein fro

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17

Okumura, Hisashi, та Satoru G. Itoh. "Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation". Molecules 27, № 8 (2022): 2483. http://dx.doi.org/10.3390/molecules27082483.

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Alzheimer’s disease is understood to be caused by amyloid fibrils and oligomers formed by aggregated amyloid-β (Aβ) peptides. This review article presents molecular dynamics (MD) simulation studies of Aβ peptides and Aβ fragments on their aggregation, aggregation inhibition, amyloid fibril conformations in equilibrium, and disruption of the amyloid fibril by ultrasonic wave and infrared laser irradiation. In the aggregation of Aβ, a β-hairpin structure promotes the formation of intermolecular β-sheet structures. Aβ peptides tend to exist at hydrophilic/hydrophobic interfaces and form more β-ha

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18

Wickner, Reed B., Herman K. Edskes, David A. Bateman, et al. "Amyloid diseases of yeast: prions are proteins acting as genes." Essays in Biochemistry 56 (August 18, 2014): 193–205. http://dx.doi.org/10.1042/bse0560193.

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The unusual genetic properties of the non-chromosomal genetic elements [URE3] and [PSI+] led to them being identified as prions (infectious proteins) of Ure2p and Sup35p respectively. Ure2p and Sup35p, and now several other proteins, can form amyloid, a linear ordered polymer of protein monomers, with a part of each molecule, the prion domain, forming the core of this β-sheet structure. Amyloid filaments passed to a new cell seed the conversion of the normal form of the protein into the same amyloid form. The cell's phenotype is affected, usually from the deficiency of the normal form of the p

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19

LeVine, Harry. "Thioflavine T interaction with amyloid β-sheet structures". Amyloid 2, № 1 (1995): 1–6. http://dx.doi.org/10.3109/13506129509031881.

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20

Fändrich, Marcus, Matthias Schmidt та Nikolaus Grigorieff. "Recent progress in understanding Alzheimer's β-amyloid structures". Trends in Biochemical Sciences 36, № 6 (2011): 338–45. http://dx.doi.org/10.1016/j.tibs.2011.02.002.

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21

Xie, Longsheng, Christopher Lockhart, Steven R. Bowers, Dmitri K. Klimov та Mohsin Saleet Jafri. "Structural Analysis of Amylin and Amyloid β Peptide Signaling in Alzheimer’s Disease". Biomolecules 15, № 1 (2025): 89. https://doi.org/10.3390/biom15010089.

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Amylin and amyloid β belong to the same protein family and activate the same receptors. Amyloid β levels are elevated in Alzheimer’s disease. Recent studies have demonstrated that amylin-based peptides can reduce the symptoms of Alzheimer’s disease in animal models. Replica exchange molecular dynamics simulation machine learning, as well as other computational analyses, were applied to improve the understanding of the amino acid residues in these amylin-based peptides. Comparisons were made between amylin, amylin-based peptides, and amyloid β. These studies converged on amylin residues 10Q, 28

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22

Gorman, Paul M., та Avijit Chakrabartty. "Alzheimer β-amyloid peptides: Structures of amyloid fibrils and alternate aggregation products". Biopolymers 60, № 5 (2001): 381. http://dx.doi.org/10.1002/1097-0282(2001)60:5<381::aid-bip10173>3.0.co;2-u.

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23

Chimon, Sandra, Medhat A. Shaibat, Christopher R. Jones, Diana C. Calero, Buzulagu Aizezi та Yoshitaka Ishii. "Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid". Nature Structural & Molecular Biology 14, № 12 (2007): 1157–64. http://dx.doi.org/10.1038/nsmb1345.

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24

Willem, Michael, та Marcus Fändrich. "A molecular view of human amyloid-β folds". Science 375, № 6577 (2022): 147–48. http://dx.doi.org/10.1126/science.abn5428.

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25

Daskalov, Asen, Denis Martinez, Virginie Coustou, et al. "Structural and molecular basis of cross-seeding barriers in amyloids." Proceedings of the National Academy of Sciences 118, no. 1 (2020): e2014085118. http://dx.doi.org/10.1073/pnas.2014085118.

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Neurodegenerative disorders are frequently associated with β-sheet-rich amyloid deposits. Amyloid-forming proteins can aggregate under different structural conformations known as strains, which can exhibit a prion-like behavior and distinct pathophenotypes. Precise molecular determinants defining strain specificity and cross-strain interactions (cross-seeding) are currently unknown. The HET-s prion protein from the fungusPodospora anserinarepresents a model system to study the fundamental properties of prion amyloids. Here, we report the amyloid prion structure of HELLF, a distant homolog of t

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Roterman, Irena, Katarzyna Stapor, and Leszek Konieczny. "Secondary Structure in Amyloids in Relation to Their Wild Type Forms." International Journal of Molecular Sciences 24, no. 1 (2022): 154. http://dx.doi.org/10.3390/ijms24010154.

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The amyloid structures and their wild type forms, available in the PDB database, provide the basis for comparative analyses. Globular proteins are characterised by a 3D spatial structure, while a chain in any amyloid fibril has a 2D structure. Another difference lies in the structuring of the hydrogen bond network. Amyloid forms theoretically engage all the NH and C=O groups of the peptide bonds in a chain with two hydrogen bonds each. In addition, the hydrogen bond network is highly ordered—as perpendicular to the plane of the chain. The β-structure segments provide the hydrogen bond system w

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Jara-Moreno, Daniela, Ana L. Riveros, Andrés Barriga, Marcelo J. Kogan та Carla Delporte. "Inhibition of β-amyloid Aggregation of Ugni molinae Extracts". Current Pharmaceutical Design 26, № 12 (2020): 1365–76. http://dx.doi.org/10.2174/1381612826666200113160840.

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The β-amyloid peptide (1-42) is a molecule capable of aggregating into neurotoxic structures that have been implicated as potential etiological factors of Alzheimer's Disease. The aim of this study was to evaluate the inhibition of β-amyloid aggregation of ethyl acetate and ethanolic extracts obtained from Ugni molinae leaves on neurotoxic actions of β-amyloid aggregates. Chemical analyses were carried out with the extracts in order to determine their phenolic profile and its quantification. Both extracts showed a tendency to reduce neuronal deaths caused by β-amyloid. This tendency was invers

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Tavanti, Francesco, Alfonso Pedone та Maria Cristina Menziani. "Disclosing the Interaction of Gold Nanoparticles with Aβ(1–40) Monomers through Replica Exchange Molecular Dynamics Simulations". International Journal of Molecular Sciences 22, № 1 (2020): 26. http://dx.doi.org/10.3390/ijms22010026.

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Amyloid-β aggregation is one of the principal causes of amyloidogenic diseases that lead to the loss of neuronal cells and to cognitive impairments. The use of gold nanoparticles treating amyloidogenic diseases is a promising approach, because the chemistry of the gold surface can be tuned in order to have a specific binding, obtaining effective tools to control the aggregation. In this paper, we show, by means of Replica Exchange Solute Tempering Molecular Simulations, how electrostatic interactions drive the absorption of Amyloid-β monomers onto citrates-capped gold nanoparticles. Importantl

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29

Serpell, Louise. "Amyloid structure." Essays in Biochemistry 56 (August 18, 2014): 1–10. http://dx.doi.org/10.1042/bse0560001.

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Amyloid fibrils are formed by numerous proteins and peptides that share little sequence homology. The structures formed are highly ordered and extremely stable, being composed of β-sheet structure and stabilized along their length by hydrogen bonding. The fibrils are formed by several protofilaments that wind around one another in rope-like structures, lending further strength and stability to the resulting fibres. The fact that so many proteins and peptides form amyloid structures under suitable conditions, seems to suggest that the sequence of the precursor is unimportant. However, it is now

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Urban, Jennifer M., Janson Ho, Gavin Piester, Riqiang Fu та Bradley L. Nilsson. "Rippled β-Sheet Formation by an Amyloid-β Fragment Indicates Expanded Scope of Sequence Space for Enantiomeric β-Sheet Peptide Coassembly". Molecules 24, № 10 (2019): 1983. http://dx.doi.org/10.3390/molecules24101983.

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In 1953, Pauling and Corey predicted that enantiomeric β-sheet peptides would coassemble into so-called “rippled” β-sheets, in which the β-sheets would consist of alternating l- and d-peptides. To date, this phenomenon has been investigated primarily with amphipathic peptide sequences composed of alternating hydrophilic and hydrophobic amino acid residues. Here, we show that enantiomers of a fragment of the amyloid-β (Aβ) peptide that does not follow this sequence pattern, amyloid-β (16–22), readily coassembles into rippled β-sheets. Equimolar mixtures of enantiomeric amyloid-β (16–22) peptide

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31

Pellegrino, S., N. Tonali, E. Erba та ін. "β-Hairpin mimics containing a piperidine–pyrrolidine scaffold modulate the β-amyloid aggregation process preserving the monomer species". Chemical Science 8, № 2 (2017): 1295–302. http://dx.doi.org/10.1039/c6sc03176e.

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TJERNBERG, Lars O., Agneta TJERNBERG, Niklas BARK та ін. "Assembling amyloid fibrils from designed structures containing a significant amyloid β-peptide fragment". Biochemical Journal 366, № 1 (2002): 343–51. http://dx.doi.org/10.1042/bj20020229.

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The amyloid plaque, consisting of amyloid β-peptide (Aβ) fibrils surrounded by dystrophic neurites, is an invariable feature of Alzheimer's disease. The determination of the molecular structure of Aβ fibrils is a significant goal that may lead to the structure-based design of effective therapeutics for Alzheimer's disease. Technical challenges have thus far rendered this goal impossible. In the present study, we develop an alternative methodology. Rather than determining the structure directly, we design conformationally constrained peptides and demonstrate that only certain ‘bricks’ can aggre

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Muvva, Charuvaka, Natarajan Arul Murugan, and Venkatesan Subramanian. "Assessment of Amyloid Forming Tendency of Peptide Sequences from Amyloid Beta and Tau Proteins Using Force-Field, Semi-Empirical, and Density Functional Theory Calculations." International Journal of Molecular Sciences 22, no. 6 (2021): 3244. http://dx.doi.org/10.3390/ijms22063244.

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A wide variety of neurodegenerative diseases are characterized by the accumulation of protein aggregates in intraneuronal or extraneuronal brain regions. In Alzheimer’s disease (AD), the extracellular aggregates originate from amyloid-β proteins, while the intracellular aggregates are formed from microtubule-binding tau proteins. The amyloid forming peptide sequences in the amyloid-β peptides and tau proteins are responsible for aggregate formation. Experimental studies have until the date reported many of such amyloid forming peptide sequences in different proteins, however, there is still li

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Folmert, Kristin, Malgorzata Broncel, Hans v. Berlepsch, Christopher Hans Ullrich, Mary-Ann Siegert, and Beate Koksch. "Inhibition of peptide aggregation by means of enzymatic phosphorylation." Beilstein Journal of Organic Chemistry 12 (November 18, 2016): 2462–70. http://dx.doi.org/10.3762/bjoc.12.240.

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As is the case in numerous natural processes, enzymatic phosphorylation can be used in the laboratory to influence the conformational populations of proteins. In nature, this information is used for signal transduction or energy transfer, but has also been shown to play an important role in many diseases like tauopathies or diabetes. With the goal of determining the effect of phosphorylation on amyloid fibril formation, we designed a model peptide which combines structural characteristics of α-helical coiled-coils and β-sheets in one sequence. This peptide undergoes a conformational transition

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Almeida, Zaida L., and Rui M. M. Brito. "Amyloid Disassembly: What Can We Learn from Chaperones?" Biomedicines 10, no. 12 (2022): 3276. http://dx.doi.org/10.3390/biomedicines10123276.

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Protein aggregation and subsequent accumulation of insoluble amyloid fibrils with cross-β structure is an intrinsic characteristic of amyloid diseases, i.e., amyloidoses. Amyloid formation involves a series of on-pathway and off-pathway protein aggregation events, leading to mature insoluble fibrils that eventually accumulate in multiple tissues. In this cascade of events, soluble oligomeric species are formed, which are among the most cytotoxic molecular entities along the amyloid cascade. The direct or indirect action of these amyloid soluble oligomers and amyloid protofibrils and fibrils in

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Westlind-Danielsson, Anita, та Gunnel Arnerup. "Spontaneous in Vitro Formation of Supramolecular β-Amyloid Structures, “βamy Balls”, by β-Amyloid 1−40 Peptide†". Biochemistry 40, № 49 (2001): 14736–43. http://dx.doi.org/10.1021/bi010375c.

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Murakoshi, Yuko, Tsuyoshi Takahashi та Hisakazu Mihara. "Modification of a Small β-Barrel Protein, To Give Pseudo-Amyloid Structures, Inhibits Amyloid β-Peptide Aggregation". Chemistry - A European Journal 19, № 14 (2013): 4525–31. http://dx.doi.org/10.1002/chem.201202762.

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Ábrahám, Ágnes, Flavio Massignan, Gergő Gyulai, Miklós Katona, Nóra Taricska, and Éva Kiss. "Comparative Study of the Solid-Liquid Interfacial Adsorption of Proteins in Their Native and Amyloid Forms." International Journal of Molecular Sciences 23, no. 21 (2022): 13219. http://dx.doi.org/10.3390/ijms232113219.

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The adhesive properties of amyloid fibers are thought to play a crucial role in various negative and positive aggregation processes, the study of which might help in their understanding and control. Amyloids have been prepared from two proteins, lysozyme and β-lactoglobulin, as well as an Exendin-4 derivative miniprotein (E5). Thermal treatment was applied to form amyloids and their structure was verified by thioflavin T (ThT), 8-Anilino-1-naphthalenesulfonic acid (ANS) dye tests and electronic circular dichroism spectroscopy (ECD). Adsorption properties of the native and amyloid forms of the

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Pusara, Srdjan. "Molecular Dynamics Insights into the Aggregation Behavior of N-Terminal β-Lactoglobulin Peptides". International Journal of Molecular Sciences 25, № 9 (2024): 4660. http://dx.doi.org/10.3390/ijms25094660.

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β-lactoglobulin (BLG) forms amyloid-like aggregates at high temperatures, low pH, and low ionic strengths. At a pH below 2, BLG undergoes hydrolysis into peptides, with N-terminal peptides 1–33 and 1–52 being prone to fibrillization, forming amyloid-like fibrils. Due to their good mechanical properties, BLG amyloids demonstrate great potential for diverse applications, including biosensors, nanocomposites, and catalysts. Consequently, further studies are essential to comprehensively understand the factors governing the formation of BLG amyloid-like morphologies. In this study, all-atom molecul

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Tycko, Robert, Kimberly L. Sciarretta, Joseph P. R. O. Orgel та Stephen C. Meredith. "Evidence for Novel β-Sheet Structures in Iowa Mutant β-Amyloid Fibrils". Biochemistry 48, № 26 (2009): 6072–84. http://dx.doi.org/10.1021/bi9002666.

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Zhizhin, Gennadiy Vladimirovich. "On the Possible Spatial Structures of the β-Amyloid". International Journal of Applied Research on Public Health Management 7, № 1 (2022): 1–8. http://dx.doi.org/10.4018/ijarphm.290380.

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Spatial models of the β - structures of protein molecules, forming layers of amino acids, in principle, of unlimited length for both antiparallel and parallel conformation have been constructed. It is shown that the simplified flat Pauling models do not reflect the spatial structure of these layers. Using the recently developed theory of higher-dimensional polytopic prismahedrons, models of the volumetric filling of space with amino acid molecules are constructed. The constructed models for the first time mathematically describe the native structures of globular proteins.

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Pham, Johnny D., Nicholas Chim, Celia W. Goulding та James S. Nowick. "Structures of Oligomers of a Peptide from β-Amyloid". Journal of the American Chemical Society 135, № 33 (2013): 12460–67. http://dx.doi.org/10.1021/ja4068854.

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Morris, Kyle L., Alison Rodger, Matthew R. Hicks, et al. "Exploring the sequence–structure relationship for amyloid peptides." Biochemical Journal 450, no. 2 (2013): 275–83. http://dx.doi.org/10.1042/bj20121773.

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Amyloid fibril formation is associated with misfolding diseases, as well as fulfilling a functional role. The cross-β molecular architecture has been reported in increasing numbers of amyloid-like fibrillar systems. The Waltz algorithm is able to predict ordered self-assembly of amyloidogenic peptides by taking into account the residue type and position. This algorithm has expanded the amyloid sequence space, and in the present study we characterize the structures of amyloid-like fibrils formed by three peptides identified by Waltz that form fibrils but not crystals. The structural challenge i

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Lipke, Peter N., Marion Mathelié-Guinlet, Albertus Viljoen, and Yves F. Dufrêne. "A New Function for Amyloid-Like Interactions: Cross-Beta Aggregates of Adhesins form Cell-to-Cell Bonds." Pathogens 10, no. 8 (2021): 1013. http://dx.doi.org/10.3390/pathogens10081013.

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Amyloid structures assemble through a repeating type of bonding called “cross-β”, in which identical sequences in many protein molecules form β-sheets that interdigitate through side chain interactions. We review the structural characteristics of such bonds. Single cell force microscopy (SCFM) shows that yeast expressing Als5 adhesin from Candida albicans demonstrate the empirical characteristics of cross-β interactions. These properties include affinity for amyloid-binding dyes, birefringence, critical concentration dependence, repeating structure, and inhibition by anti-amyloid agents. We pr

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Sønderby, Thorbjørn Vincent, Zahra Najarzadeh, and Daniel Erik Otzen. "Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies." Molecules 27, no. 13 (2022): 4080. http://dx.doi.org/10.3390/molecules27134080.

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Functional amyloid is produced by many organisms but is particularly well understood in bacteria, where proteins such as CsgA (E. coli) and FapC (Pseudomonas) are assembled as functional bacterial amyloid (FuBA) on the cell surface in a carefully optimized process. Besides a host of helper proteins, FuBA formation is aided by multiple imperfect repeats which stabilize amyloid and streamline the aggregation mechanism to a fast-track assembly dominated by primary nucleation. These repeats, which are found in variable numbers in Pseudomonas, are most likely the structural core of the fibrils, tho

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Lee, Myungwoon, Tuo Wang, Olga V. Makhlynets, et al. "Zinc-binding structure of a catalytic amyloid from solid-state NMR." Proceedings of the National Academy of Sciences 114, no. 24 (2017): 6191–96. http://dx.doi.org/10.1073/pnas.1706179114.

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Throughout biology, amyloids are key structures in both functional proteins and the end product of pathologic protein misfolding. Amyloids might also represent an early precursor in the evolution of life because of their small molecular size and their ability to self-purify and catalyze chemical reactions. They also provide attractive backbones for advanced materials. When β-strands of an amyloid are arranged parallel and in register, side chains from the same position of each chain align, facilitating metal chelation when the residues are good ligands such as histidine. High-resolution struct

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Diaferia, Carlo, Nicole Balasco, Davide Altamura, et al. "Assembly modes of hexaphenylalanine variants as function of the charge states of their terminal ends." Soft Matter 14, no. 40 (2018): 8219–30. http://dx.doi.org/10.1039/c8sm01441h.

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Lomarat, Pattamapan, Sirirat Chancharunee, Natthinee Anantachoke, Worawan Kitphati, Kittisak Sripha, and Nuntavan Bunyapraphatsara. "Bioactivity-guided Separation of the Active Compounds in Acacia Pennata Responsible for the Prevention of Alzheimer's Disease." Natural Product Communications 10, no. 8 (2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000830.

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The objective of this study was to evaluate the health benefits of plants used in Thai food, specifically Acacia pennata Willd., in Alzheimer's prevention. A. pennata twigs strongly inhibited β-amyloid aggregation. Bioactivity-guided separation of the active fractions yielded six known compounds, tetracosane (1), 1-(heptyloxy)-octadecane (2), methyl tridecanoate (3), arborinone (4), confertamide A (5) and 4-hydroxy-1-methyl-pyrrolidin-2-carboxylic acid (6). The structures were determined by spectroscopic analysis. Biological testing revealed that tetracosane (1) was the most potent inhibitor o

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Flores-Fernández, José, Vineet Rathod, and Holger Wille. "Comparing the Folds of Prions and Other Pathogenic Amyloids." Pathogens 7, no. 2 (2018): 50. http://dx.doi.org/10.3390/pathogens7020050.

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Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt–Jakob disease, Alzheimer’s disease, and Parkinson’s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-β(1-42) (Aβ(1-42)) fibrils, and α-synuclein fibrils were recently reported using cryo-electron microscopy. A high-resolution structure for the infectious prion protein, PrPSc, is not yet available due to its insolubility and its propensity to aggregate, but cryo-electron microscopy, X-ray fiber diffraction, and other approaches have defined the overall architec

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Cohen, Mark L., Chae Kim, Tracy Haldiman та ін. "Rapidly progressive Alzheimer’s disease features distinct structures of amyloid-β". Brain 138, № 4 (2015): 1009–22. http://dx.doi.org/10.1093/brain/awv006.

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