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Journal articles on the topic 'Fibrils'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

Hagg, Rupert, Peter Bruckner, and Erik Hedbom. "Cartilage Fibrils of Mammals are Biochemically Heterogeneous: Differential Distribution of Decorin and Collagen IX." Journal of Cell Biology 142, no. 1 (1998): 285–94. http://dx.doi.org/10.1083/jcb.142.1.285.

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Cartilage fibrils contain collagen II as the major constituent, but the presence of additional components, minor collagens, and noncollagenous glycoproteins is thought to be crucial for modulating several fibril properties. We have examined the distribution of two fibril constituents—decorin and collagen IX—in samples of fibril fragments obtained after bovine cartilage homogenization. Decorin was preferentially associated with a population of thicker fibril fragments from adult articular cartilage, but was not present on the thinnest fibrils. The binding was specific for the gap regions of the

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2

Karunarathne, Kanchana, Nabila Bushra, Olivia Williams, et al. "Self-Assembly of Amyloid Fibrils Into 3D Gel Clusters Versus 2D Sheets." Biomolecules 13, no. 2 (2023): 230. http://dx.doi.org/10.3390/biom13020230.

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The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human disorders, including many neurodegenerative diseases. Fibril plaques are predominately composed of amyloid fibrils, characterized by their underlying cross beta-sheet architecture. Research into the mechanisms of amyloid formation has mostly focused on characterizing and modeling the growth of individual fibrils and associated oligomers from their monomeric precursors. Much less is known about the mechanisms causing individual fibrils to assemble into ordered fibrillar suprastructures. Elucidat

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3

Murvai, Ünige, Judit Somkuti, László Smeller, Botond Penke та Miklós SZ Kellermayer. "Structural and nanomechanical comparison of epitaxially and solution-grown amyloid β25-35 fibrils." Biochim Biophys Acta. 1854, № 5 (2015): 327–32. https://doi.org/10.1016/j.bbapap.2015.01.003.

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Aβ25-35, the fibril-forming, biologically active toxic fragment of the full-length amyloid β-peptide also forms fibrils on mica by an epitaxial assembly mechanism. Here we investigated, by using atomic force microscopy, nanomechanical manipulation and FTIR spectroscopy, whether the epitaxially grown fibrils display structural and mechanical features similar to the ones evolving under equilibrium conditions in bulk solution. Unlike epitaxially grown fibrils, solution-grown fibrils displayed a heterogeneous morphology and an apparently helical structure. While fibril assembly in soluti

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4

Liu, Yehe, Nelly Andarawis-Puri, and Steven J. Eppell. "Method to extract minimally damaged collagen fibrils from tendon." Journal of Biological Methods 3, no. 4 (2016): e54. http://dx.doi.org/10.14440/jbm.2016.121.

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A new method is presented to extract collagen fibrils from mammalian tendon tissue. Mammalian tendons are treated with a trypsin-based extraction medium and gently separated with tweezers in an aqueous solution. Collagen fibrils released in the solution are imaged using both dark-field light microscopy and scanning electron microscopy. The method successfully extracts isolated fibrils from rat tail and patellar tendons. To examine whether the method is likely to damage fibrils during extraction, sea cucumber dermis fibril lengths are compared against those obtained using only distilled water.

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Milton, Nathaniel G. N., and J. Robin Harris. "Human Islet Amyloid Polypeptide Fibril Binding to Catalase: A Transmission Electron Microscopy and Microplate Study." Scientific World JOURNAL 10 (2010): 879–93. http://dx.doi.org/10.1100/tsw.2010.73.

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The diabetes-associated human islet amyloid polypeptide (IAPP) is a 37-amino-acid peptide that forms fibrilsin vitroandin vivo. Human IAPP fibrils are toxic in a similar manner to Alzheimer's amyloid-β (Aβ) and prion protein (PrP) fibrils. Previous studies have shown that catalase binds to Aβ fibrils and appears to recognize a region containing the Gly-Ala-Ile-Ile sequence that is similar to the Gly-Ala-Ile-Leu sequence found in human IAPP residues 24-27. This study presents a transmission electron microscopy (TEM)—based analysis of fibril formation and the binding of human erythrocyte catalas

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6

Carapeto, Ana P., Carlos Marcuello, Patrícia F. N. Faísca, and Mário S. Rodrigues. "Morphological and Biophysical Study of S100A9 Protein Fibrils by Atomic Force Microscopy Imaging and Nanomechanical Analysis." Biomolecules 14, no. 9 (2024): 1091. http://dx.doi.org/10.3390/biom14091091.

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Atomic force microscopy (AFM) imaging enables the visualization of protein molecules with high resolution, providing insights into their shape, size, and surface topography. Here, we use AFM to study the aggregation process of protein S100A9 in physiological conditions, in the presence of calcium at a molar ratio 4Ca2+:S100A9. We find that S100A9 readily assembles into a worm-like fibril, with a period dimension along the fibril axis of 11.5 nm. The fibril’s chain length extends up to 136 periods after an incubation time of 144 h. At room temperature, the fibril’s bending stiffness was found t

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Pradhan, Tejaswini, Karthikeyan Annamalai, Riddhiman Sarkar та ін. "Seeded fibrils of the germline variant of human λ-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability". Journal of Biological Chemistry 295, № 52 (2020): 18474–84. http://dx.doi.org/10.1074/jbc.ra120.016006.

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Systemic antibody light chains (AL) amyloidosis is characterized by deposition of amyloid fibrils derived from a particular antibody light chain. Cardiac involvement is a major risk factor for mortality. Using MAS solid-state NMR, we studied the fibril structure of a recombinant light chain fragment corresponding to the fibril protein from patient FOR005, together with fibrils formed by protein sequence variants that are derived from the closest germline (GL) sequence. Both analyzed fibril structures were seeded with ex-vivo amyloid fibrils purified from the explanted heart of this patient. We

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8

Winklbauer, R., and C. Stoltz. "Fibronectin fibril growth in the extracellular matrix of the Xenopus embryo." Journal of Cell Science 108, no. 4 (1995): 1575–86. http://dx.doi.org/10.1242/jcs.108.4.1575.

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We show that the mechanism of fibronectin fibril formation on the blastocoel roof of the Xenopus embryo is comparable to that in other systems. Fibril assembly is inhibited by RGD peptide, by an amino-terminal fragment of fibronectin, and by cytochalasin B. When added exogenously, intact fibronectin, but not a 110 kDa cell binding fragment of fibronectin, is incorporated into fibrils. Thus, the blastocoel roof of Xenopus represents a valid model system for the study of fibronectin fibril formation in situ. Moreover, we show that fibril formation can be induced experimentally in this system. Ex

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9

KADLER, Karl E., David F. HOLMES, John A. TROTTER, and John A. CHAPMAN. "Collagen fibril formation." Biochemical Journal 316, no. 1 (1996): 1–11. http://dx.doi.org/10.1042/bj3160001.

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Collagen is most abundant in animal tissues as very long fibrils with a characteristic axial periodic structure. The fibrils provide the major biomechanical scaffold for cell attachment and anchorage of macromolecules, allowing the shape and form of tissues to be defined and maintained. How the fibrils are formed from their monomeric precursors is the primary concern of this review. Collagen fibril formation is basically a self-assembly process (i.e. one which is to a large extent determined by the intrinsic properties of the collagen molecules themselves) but it is also sensitive to cell-medi

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10

Nakata, Yui, Yuuto Kitazaki, Hitomi Kanaoka, et al. "Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from Escherichia coli." International Journal of Molecular Sciences 23, no. 21 (2022): 13243. http://dx.doi.org/10.3390/ijms232113243.

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The molecular chaperones HdeA and HdeB of the Escherichia coli (E. coli) periplasm protect client proteins from acid denaturation through a unique mechanism that utilizes their acid denatured states to bind clients. We previously demonstrated that the active, acid-denatured form of HdeA is also prone to forming inactive, amyloid fibril-like aggregates in a pH-dependent, reversible manner. In this study, we report that HdeB also displays a similar tendency to form fibrils at low pH. HdeB fibrils were observed at pH < 3 in the presence of NaCl. Similar to HdeA, HdeB fibrils could be resolubil

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11

Noskov, Boris, Giuseppe Loglio, Reinhard Miller, Olga Milyaeva, Maria Panaeva та Alexey Bykov. "Dynamic Surface Properties of α-Lactalbumin Fibril Dispersions". Polymers 15, № 19 (2023): 3970. http://dx.doi.org/10.3390/polym15193970.

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The dynamic surface properties of aqueous dispersions of α-lactalbumin (ALA) amyloid fibrils differ noticeably from the properties of the fibril dispersions of other globular proteins. As a result, the protocol of the application of ALA fibrils to form stable foams and emulsions has to be deviate from that of other protein fibrils. Unlike the fibrils of β-lactoglobulin and lysozyme, ALA fibrils can be easily purified from hydrolyzed peptides and native protein molecules. The application of the oscillating barrier method shows that the dynamic surface elasticity of ALA fibril dispersions exceed

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12

Teangtam, Sarocha, Wissanee Yingprasert, and Phichit Somboon. "Production of micro-lignocellulosic fibril rubber composites and their application in coated layers of building materials." BioResources 19, no. 1 (2023): 620–34. http://dx.doi.org/10.15376/biores.19.1.620-634.

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Novel composite materials were made by combining micro-lignocellulosic fibrils and natural rubber applied as spray coated layers for building materials. The micro-lignocellulosic fibrils were produced based on the mechanical pulping process with jute bast as the raw material. The obtained micro-lignocellulosic fibrils had a good content of water-suspended materials with fibril widths of about 0.1 to 1.0 µm and fibril length of about 100 to 150 µm. The composites were produced using natural rubber mixed with the micro-lignocellulosic fibrils at 0, 5, and 10 parts per hundred of rubber, vulcaniz

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13

Li, Jinqing, Zichao Yang, Han Liu, et al. "ADS-J1 disaggregates semen-derived amyloid fibrils." Biochemical Journal 476, no. 6 (2019): 1021–35. http://dx.doi.org/10.1042/bcj20180886.

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Abstract Semen-derived amyloid fibrils, comprising SEVI (semen-derived enhancer of viral infection) fibrils and SEM1 fibrils, could remarkably enhance HIV-1 sexual transmission and thus are potential targets for the development of an effective microbicide. Previously, we found that ADS-J1, apart from being an HIV-1 entry inhibitor, could also potently inhibit seminal amyloid fibrillization and block fibril-mediated enhancement of viral infection. However, the remodeling effects of ADS-J1 on mature seminal fibrils were unexplored. Herein, we investigated the capacity of ADS-J1 to disassemble se

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14

Sandhya A, Gomathi Kanayiram, Kiruthika L, and Aafreen Afroz S. "Nigella Sativa : A Potential Inhibitor for Insulin Fibril Formation." International Journal of Research in Pharmaceutical Sciences 11, no. 1 (2020): 765–74. http://dx.doi.org/10.26452/ijrps.v11i1.1891.

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The high order structure from proteins which are self-assembled are known as fibrils. They are collectively called as amyloid fibrils, which generally lead to neurodegenerative diseases like Alzheimer's, Parkinson's, Huntington's, Type II diabetes. Insulin fibril aggregation is identified to be the major cause of neurodegenerative diseases. The effect of Nigella sativa extract is analyzed based on the fibril inhibition process. The formed fibrils is reduced with the concentration increase of Nigella sativa extract. Insulin fibril is found in Type II diabetes patients after repeated insulin inj

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15

Anan, Intissar, Ole B. Suhr, Katarzyna Liszewska, et al. "Amyloid fibril composition type is consistent over time in patients with Val30Met (p.Val50Met) transthyretin amyloidosis." PLOS ONE 17, no. 3 (2022): e0266092. http://dx.doi.org/10.1371/journal.pone.0266092.

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Background We have previously shown that transthyretin (TTR) amyloidosis patients have amyloid fibrils of either of two compositions; type A fibrils consisting of large amounts of C-terminal TTR fragments in addition to full-length TTR, or type B fibrils consisting of only full-length TTR. Since type A fibrils are associated with an older age in ATTRVal30Met (p.Val50Met) amyloidosis patients, it has been discussed if the TTR fragments are derived from degradation of the amyloid deposits as the patients are aging. The present study aimed to investigate if the fibril composition type changes ove

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16

Behnke, O. "Platelet Adhesion to Native Collagens Involves Proteoglycans and May Be a Two-Step Process." Thrombosis and Haemostasis 58, no. 02 (1987): 786–89. http://dx.doi.org/10.1055/s-0038-1645970.

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SummaryAdhesion of rat blood platelets to native rat tail collagen fibrils was studied in the electron microscope under conditions that preserved collagen-associated proteoglycans (CAPG). The CAPG molecules were aligned in chain-like configurations that encircled the fibrils with a 65 nm period; they appeared to coat the fibrils completely and extended 60-100 nm away from the fibril. The initial platelet-fibril contact occurred between the platelet glycocalyx and the CAPG of the fibrils i.e. between two surfaces with net-negative charges. When close contact was established between the fibril s

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17

Selivanova, O. M., V. V. Rogachevsky, A. K. Syrin, and O. V. Galzitskaya. "Molecular mechanism of amyloid formation by Ab peptide: review of own works." Biomeditsinskaya Khimiya 64, no. 1 (2018): 94–109. http://dx.doi.org/10.18097/pbmc20186401094.

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TA characteristic feature of amyloid structures is polymorphism. The study of amyloid structures and their formation process was carried out for synthetic and recombinant Ab(1-40) and Ab(1-42) peptide preparations. In the study of these peptides, we recognized fibrils of different morphologies. We observed fibrillar formations in the form of single fibrils, ribbons, bundles, bunches, and clusters. Polymorphism of fibrils was observed not only when the environmental conditions changed, but under the same conditions and this was a common characteristics of all amyloid formations. Fibrils of Ab(1

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18

Galzitskaya, Oxana. "New Mechanism of Amyloid Fibril Formation." Current Protein & Peptide Science 20, no. 6 (2019): 630–40. http://dx.doi.org/10.2174/1389203720666190125160937.

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Polymorphism is a specific feature of the amyloid structures. We have studied the amyloid structures and the process of their formation using the synthetic and recombinant preparations of Aβ peptides and their three fragments. The fibrils of different morphology were obtained for these peptides. We suppose that fibril formation by Aβ peptides and their fragments proceeds according to the simplified scheme: destabilized monomer → ring-like oligomer → mature fibril that consists of ringlike oligomers. We are the first who did 2D reconstruction of amyloid fibrils provided that just a ringlike oli

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19

Birk, D. E., J. M. Fitch, J. P. Babiarz, and T. F. Linsenmayer. "Collagen type I and type V are present in the same fibril in the avian corneal stroma." Journal of Cell Biology 106, no. 3 (1988): 999–1008. http://dx.doi.org/10.1083/jcb.106.3.999.

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The distribution, supramolecular form, and arrangement of collagen types I and V in the chicken embryo corneal stroma were studied using electron microscopy, collagen type-specific monoclonal antibodies, and a preembedding immunogold method. Double-label immunoelectron microscopy with colloidal gold-tagged monoclonal antibodies was used to simultaneously localize collagen type I and type V within the chick corneal stroma. The results definitively demonstrate, for the first time, that both collagens are codistributed within the same fibril. Type I collagen was localized to striated fibrils thro

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20

Kang, Ning, Jin Hua, Lizhen Gao, Bin Zhang, and Jiewen Pang. "The Interplay between Whey Protein Fibrils with Carbon Nanotubes or Carbon Nano-Onions." Materials 14, no. 3 (2021): 608. http://dx.doi.org/10.3390/ma14030608.

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Whey protein isolate (WPI) fibrils were prepared using an acid hydrolysis induction process. Carbon nanotubes (CNTs) and carbon nano-onions (CNOs) were made via the catalytic chemical vapor deposition (CVD) of methane. WPI fibril–CNTs and WPI fibril–CNOs were prepared via hydrothermal synthesis at 80 °C. The composites were characterized by SEM, TEM, FTIR, XRD, Raman, and TG analyses. The interplay between WPI fibrils and CNTs and CNOs were studied. The WPI fibrils with CNTs and CNOs formed uniform gels and films. CNTs and CNOs were highly dispersed in the gels. Hydrogels of WPI fibrils with C

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21

Cheng, Qinghui, Zhi-Wen Hu, Yuto Tobin-Miyaji, Amy E. Perkins, Terrence Deak та Wei Qiang. "Fibrillization of 40-residue β-Amyloid Peptides in Membrane-Like Environments Leads to Different Fibril Structures and Reduced Molecular Polymorphisms". Biomolecules 10, № 6 (2020): 881. http://dx.doi.org/10.3390/biom10060881.

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The molecular-level polymorphism in β-Amyloid (Aβ) fibrils have recently been considered as a pathologically relevant factor in Alzheimer’s disease (AD). Studies showed that the structural deviations in human-brain-seeded Aβ fibrils potentially correlated with the clinical histories of AD patients. For the 40-residue Aβ (Aβ40) fibrils derived from human brain tissues, a predominant molecular structure was proposed based on solid-state nuclear magnetic resonance (ssNMR) spectroscopy. However, previous studies have shown that the molecular structures of Aβ40 fibrils were sensitive to their growt

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22

Norris, Karl, Oksana Mishukova, Agata Zykwinska, et al. "Marine Polysaccharide-Collagen Coatings on Ti6Al4V Alloy Formed by Self-Assembly." Micromachines 10, no. 1 (2019): 68. http://dx.doi.org/10.3390/mi10010068.

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Polysaccharides of marine origin are gaining interest as biomaterial components. Bacteria derived from deep-sea hydrothermal vents can produce sulfated exopolysaccharides (EPS), which can influence cell behavior. The use of such polysaccharides as components of organic, collagen fibril-based coatings on biomaterial surfaces remains unexplored. In this study, collagen fibril coatings enriched with HE800 and GY785 EPS derivatives were deposited on titanium alloy (Ti6Al4V) scaffolds produced by rapid prototyping and subjected to physicochemical and cell biological characterization. Coatings were

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23

Agopian, Audrey, та Zhefeng Guo. "Structural origin of polymorphism of Alzheimer's amyloid β-fibrils". Biochemical Journal 447, № 1 (2012): 43–50. http://dx.doi.org/10.1042/bj20120034.

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Formation of senile plaques containing amyloid fibrils of Aβ (amyloid β-peptide) is a pathological hallmark of Alzheimer's disease. Unlike globular proteins, which fold into unique structures, the fibrils of Aβ and other amyloid proteins often contain multiple polymorphs. Polymorphism of amyloid fibrils leads to different toxicity in amyloid diseases and may be the basis for prion strains, but the structural origin for fibril polymorphism is still elusive. In the present study we investigate the structural origin of two major fibril polymorphs of Aβ40: an untwisted polymorph formed under agita

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Peters, Donna M. Pesciotta, Ya Chen, Luciano Zardi, and Sara Brummel. "Conformation of Fibronectin Fibrils Varies: Discrete Globular Domains of Type III Repeats Detected." Microscopy and Microanalysis 4, no. 4 (1998): 385–96. http://dx.doi.org/10.1017/s1431927698980369.

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Cryo-high-resolution scanning electron microscopy was used to analyze the conformation of fibronectin fibrils formed in human skin fibroblast cultures or in a cell-free system by treating soluble plasma fibronectin with guanidine. Structurally, fibrils assembled in the cell-free system and in culture were similar. Assembly of both fibrillar networks involves interactions with the III1 and amino terminal repeats of fibronectin; their conformations consist of either smooth surfaces or patches of smooth surfaces and nodules randomly spaced along the fibril. The random distribution of these two co

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Watanabe-Nakayama, Takahiro, Kenjiro Ono, Masahiro Itami, Ryoichi Takahashi, David B. Teplow та Masahito Yamada. "High-speed atomic force microscopy reveals structural dynamics of amyloid β1–42 aggregates". Proceedings of the National Academy of Sciences 113, № 21 (2016): 5835–40. http://dx.doi.org/10.1073/pnas.1524807113.

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Aggregation of amyloidogenic proteins into insoluble amyloid fibrils is implicated in various neurodegenerative diseases. This process involves protein assembly into oligomeric intermediates and fibrils with highly polymorphic molecular structures. These structural differences may be responsible for different disease presentations. For this reason, elucidation of the structural features and assembly kinetics of amyloidogenic proteins has been an area of intense study. We report here the results of high-speed atomic force microscopy (HS-AFM) studies of fibril formation and elongation by the 42-

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26

Goh, K. L., J. R. Meakin, R. M. Aspden, and D. W. L. Hukins. "Influence of fibril taper on the function of collagen to reinforce extracellular matrix." Proceedings of the Royal Society B: Biological Sciences 272, no. 1575 (2005): 1979–83. http://dx.doi.org/10.1098/rspb.2005.3173.

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Collagen fibrils provide tensile reinforcement for extracellular matrix. In at least some tissues, the fibrils have a paraboloidal taper at their ends. The purpose of this paper is to determine the implications of this taper for the function of collagen fibrils. When a tissue is subjected to low mechanical forces, stress will be transferred to the fibrils elastically. This process was modelled using finite element analysis because there is no analytical theory for elastic stress transfer to a non-cylindrical fibril. When the tissue is subjected to higher mechanical forces, stress will be trans

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Marchant, J. K., R. A. Hahn, T. F. Linsenmayer, and D. E. Birk. "Reduction of type V collagen using a dominant-negative strategy alters the regulation of fibrillogenesis and results in the loss of corneal-specific fibril morphology." Journal of Cell Biology 135, no. 5 (1996): 1415–26. http://dx.doi.org/10.1083/jcb.135.5.1415.

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A number of factors have been implicated in the regulation of tissue-specific collagen fibril diameter. Previous data suggest that assembly of heterotypic fibrils composed of two different fibrillar collagens represents a general mechanism regulating fibril diameter. Specifically, we hypothesize that type V collagen is required for the assembly of the small diameter fibrils observed in the cornea. To test this, we used a dominant-negative retroviral strategy to decrease the levels of type V collagen secreted by chicken corneal fibroblasts. The chicken alpha 1(V) collagen gene was cloned, and r

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Costello, Matt, Nina Park, Alyssa Neill, et al. "Cael-101 Enhances the Clearance of Light Chain Fibrils and Intermediate Aggregates By Phagocytosis." Blood 142, Supplement 1 (2023): 3307. http://dx.doi.org/10.1182/blood-2023-186373.

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Background Light chain amyloidosis (AL) is a rare, systemic disease characterized by amyloid fibril deposition in various organs due to overproduction of light chains from plasma cell dyscrasia (PCD). Current treatment strategies target PCD rather than clearing amyloid deposits directly from organs. CAEL-101 is a chimeric monoclonal IgG1 antibody that targets these amyloid fibrils. It binds to a cryptic epitope at the N-terminus of both kappa (κ) and lambda (λ) light chain misfolded proteins. In this study we tested the role of CAEL-101 in mediating the phagocytosis of synthetic fibrils and th

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Sanami, Sarina, Tracey J. Purton, David P. Smith, Mick F. Tuite, and Wei-Feng Xue. "Comparative Analysis of the Relative Fragmentation Stabilities of Polymorphic Alpha-Synuclein Amyloid Fibrils." Biomolecules 12, no. 5 (2022): 630. http://dx.doi.org/10.3390/biom12050630.

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The division of amyloid fibril particles through fragmentation is implicated in the progression of human neurodegenerative disorders such as Parkinson’s disease. Fragmentation of amyloid fibrils plays a crucial role in the propagation of the amyloid state encoded in their three-dimensional structures and may have an important role in the spreading of potentially pathological properties and phenotypes in amyloid-associated diseases. However, despite the mechanistic importance of fibril fragmentation, the relative stabilities of different types or different polymorphs of amyloid fibrils toward f

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Sanami, Sarina, Tracey J. Purton, David P. Smith, Mick F. Tuite, and Wei-Feng Xue. "Comparative Analysis of the Relative Fragmentation Stabilities of Polymorphic Alpha-Synuclein Amyloid Fibrils." Biomolecules 12, no. 5 (2022): 630. http://dx.doi.org/10.3390/biom12050630.

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The division of amyloid fibril particles through fragmentation is implicated in the progression of human neurodegenerative disorders such as Parkinson’s disease. Fragmentation of amyloid fibrils plays a crucial role in the propagation of the amyloid state encoded in their three-dimensional structures and may have an important role in the spreading of potentially pathological properties and phenotypes in amyloid-associated diseases. However, despite the mechanistic importance of fibril fragmentation, the relative stabilities of different types or different polymorphs of amyloid fibrils toward f

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31

Sanami, Sarina, Tracey J. Purton, David P. Smith, Mick F. Tuite, and Wei-Feng Xue. "Comparative Analysis of the Relative Fragmentation Stabilities of Polymorphic Alpha-Synuclein Amyloid Fibrils." Biomolecules 12, no. 5 (2022): 630. http://dx.doi.org/10.3390/biom12050630.

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The division of amyloid fibril particles through fragmentation is implicated in the progression of human neurodegenerative disorders such as Parkinson’s disease. Fragmentation of amyloid fibrils plays a crucial role in the propagation of the amyloid state encoded in their three-dimensional structures and may have an important role in the spreading of potentially pathological properties and phenotypes in amyloid-associated diseases. However, despite the mechanistic importance of fibril fragmentation, the relative stabilities of different types or different polymorphs of amyloid fibrils toward f

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32

Mosesson, MW, JP DiOrio, KR Siebenlist, JS Wall, and JF Hainfeld. "Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction." Blood 82, no. 5 (1993): 1517–21. http://dx.doi.org/10.1182/blood.v82.5.1517.1517.

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Abstract Fibrin molecules polymerize to double-stranded fibrils by intermolecular end-to-middle domain pairing of complementary polymerization sites, accompanied by fibril branching to form a clot network. Mass/length measurements on scanning transmission electron microscopic images of fibrils comprising branch points showed two types of junctions. Tetramolecular junctions occur when two fibrils converge, creating a third branch with twice the mass/length of its constituents. Newly recognized trimolecular junctions have three fibril branches of equal mass/length, and occur when an extraneous f

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Mosesson, MW, JP DiOrio, KR Siebenlist, JS Wall, and JF Hainfeld. "Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction." Blood 82, no. 5 (1993): 1517–21. http://dx.doi.org/10.1182/blood.v82.5.1517.bloodjournal8251517.

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Fibrin molecules polymerize to double-stranded fibrils by intermolecular end-to-middle domain pairing of complementary polymerization sites, accompanied by fibril branching to form a clot network. Mass/length measurements on scanning transmission electron microscopic images of fibrils comprising branch points showed two types of junctions. Tetramolecular junctions occur when two fibrils converge, creating a third branch with twice the mass/length of its constituents. Newly recognized trimolecular junctions have three fibril branches of equal mass/length, and occur when an extraneous fibrin mol

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34

Chernii, Svitlana, Yuriy Gerasymchuk, Mykhaylo Losytskyy, et al. "Modification of insulin amyloid aggregation by Zr phthalocyanines functionalized with dehydroacetic acid derivatives." PLOS ONE 16, no. 1 (2021): e0243904. http://dx.doi.org/10.1371/journal.pone.0243904.

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Amyloid fibrils are widely studied both as target in conformational disorders and as basis for the development of protein-based functional materials. The three Zr phthalocyanines bearing dehydroacetic acid residue (PcZr(L1)2) and its condensed derivatives (PcZr(L2)2 and PcZr(L3)2) as out-of-plane ligands were synthesized and their influence on insulin fibril formation was studied by amyloid-sensitive fluorescent dye based assay, scanning electron microscopy, fluorescent and absorption spectroscopies. The presence of Zr phthalocyanines was shown to modify the fibril formation. The morphology of

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Garrison, Carly M., and Jean E. Schwarzbauer. "Fibronectin fibril alignment is established upon initiation of extracellular matrix assembly." Molecular Biology of the Cell 32, no. 8 (2021): 739–52. http://dx.doi.org/10.1091/mbc.e20-08-0533.

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Fibronectin (FN) fibril alignment is crucial for tissue function. We show that assembly of aligned fibrils is determined by the polarized localization of matrix assembly sites. Oriented sites progressed into aligned fibrillar adhesions and FN fibrils. TGF-b stimulated aligned FN assembly, providing a mechanism to modulate fibril orientation in vivo.

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Liu, Yehe, Roberto Ballarini, and Steven J. Eppell. "Tension tests on mammalian collagen fibrils." Interface Focus 6, no. 1 (2016): 20150080. http://dx.doi.org/10.1098/rsfs.2015.0080.

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A brief overview of isolated collagen fibril mechanics testing is followed by presentation of the first results testing fibrils isolated from load-bearing mammalian tendons using a microelectromechanical systems platform. The in vitro modulus (326 ± 112 MPa) and fracture stress (71 ± 23 MPa) are shown to be lower than previously measured on fibrils extracted from sea cucumber dermis and tested with the same technique. Scanning electron microscope images show the fibrils can fail with a mechanism that involves circumferential rupture, whereas the core of the fibril stays at least partially inta

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Vaughan, L., M. Mendler, S. Huber, et al. "D-periodic distribution of collagen type IX along cartilage fibrils." Journal of Cell Biology 106, no. 3 (1988): 991–97. http://dx.doi.org/10.1083/jcb.106.3.991.

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It has recently become apparent that collagen fibrils may be composed of more than one kind of macromolecule. To explore this possibility, we developed a procedure to purify fibril fragments from 17-d embryonic chicken sternal cartilage. The fibril population obtained shows, after negative staining, a uniformity in the banding pattern and diameter similar to the fibrils in situ. Pepsin digestion of this fibril preparation releases collagen types II, IX, and XI in the proportion of 8:1:1. Rotary shadowing of the fibrils reveals a d-periodic distribution of 35-40-nm long projections, each capped

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Mendler, M., S. G. Eich-Bender, L. Vaughan, K. H. Winterhalter, and P. Bruckner. "Cartilage contains mixed fibrils of collagen types II, IX, and XI." Journal of Cell Biology 108, no. 1 (1989): 191–97. http://dx.doi.org/10.1083/jcb.108.1.191.

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The distribution of collagen XI in fibril fragments from 17-d chick embryo sternal cartilage was determined by immunoelectron microscopy using specific polyclonal antibodies. The protein was distributed throughout the fibril fragments but was antigenically masked due to the tight packing of collagen molecules and could be identified only at sites where the fibril structure was partially disrupted. Collagens II and IX were also distributed uniformly along fibrils but, in contrast to collagen XI, were accessible to the antibodies in intact fibrils. Therefore, cartilage fibrils are heterotypicall

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Saelices, Lorena, Kevin Chung, Ji H. Lee, et al. "Amyloid seeding of transthyretin by ex vivo cardiac fibrils and its inhibition." Proceedings of the National Academy of Sciences 115, no. 29 (2018): E6741—E6750. http://dx.doi.org/10.1073/pnas.1805131115.

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Each of the 30 human amyloid diseases is associated with the aggregation of a particular precursor protein into amyloid fibrils. In transthyretin amyloidosis (ATTR), mutant or wild-type forms of the serum carrier protein transthyretin (TTR), synthesized and secreted by the liver, convert to amyloid fibrils deposited in the heart and other organs. The current standard of care for hereditary ATTR is liver transplantation, which replaces the mutantTTRgene with the wild-type gene. However, the procedure is often followed by cardiac deposition of wild-type TTR secreted by the new liver. Here we fin

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Buell, Alexander K. "The growth of amyloid fibrils: rates and mechanisms." Biochemical Journal 476, no. 19 (2019): 2677–703. http://dx.doi.org/10.1042/bcj20160868.

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Abstract Amyloid fibrils are β-sheet-rich linear protein polymers that can be formed by a large variety of different proteins. These assemblies have received much interest in recent decades, due to their role in a range of human disorders. However, amyloid fibrils are also found in a functional context, whereby their structural, mechanical and thermodynamic properties are exploited by biological systems. Amyloid fibrils form through a nucleated polymerisation mechanism with secondary processes acting in many cases to amplify the number of fibrils. The filamentous nature of amyloid fibrils impl

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Chai, Ya Dong, Zi Zhen Liu, Daichi Noda, and Motohiro Tagaya. "Mild Reaction of Highly-Oriented Collagen Fibril Arrays with Simulated Body Fluid." Solid State Phenomena 324 (September 20, 2021): 166–72. http://dx.doi.org/10.4028/www.scientific.net/ssp.324.166.

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The highly-oriented collagen fibrils that paralleled to one (rubbing) direction were fabricated by which the collagen molecular solution was spin-coated and self-assembled on the rubbed polyimide film. Subsequently, the hydroxyapatite crystals were precipitated on the collagen fibrils by immersing into simulated body fluid. In details, the carboxyl groups on the collagen fibrils were used as a reaction field for adsorption of Ca2+ ions and promoted the formation of hydroxyapatite crystals. As a result, the hydroxyapatite crystals grew along the a-axis leading to the formation of stable interfa

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Kelly, Jeffery W., and William E. Balch. "Amyloid as a natural product." Journal of Cell Biology 161, no. 3 (2003): 461–62. http://dx.doi.org/10.1083/jcb.200304074.

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Amyloid fibrils, such as those found in Alzheimer's and the gelsolin amyloid diseases, result from the misassembly of peptides produced by either normal or aberrant intracellular proteolytic processing. A paper in this issue by Marks and colleagues (Berson et al., 2003) demonstrates that intra-melanosome fibrils are formed through normal biological proteolytic processing of an integral membrane protein. The resulting peptide fragment assembles into fibrils promoting the formation of melanin pigment granules. These results, along with the observation that amyloid fibril formation by bacteria is

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Kaku, Toshisuke, Kaori Tsukakoshi та Kazunori Ikebukuro. "Cytotoxic Aβ Protofilaments Are Generated in the Process of Aβ Fibril Disaggregation". International Journal of Molecular Sciences 22, № 23 (2021): 12780. http://dx.doi.org/10.3390/ijms222312780.

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Significant research on Alzheimer’s disease (AD) has demonstrated that amyloid β (Aβ) oligomers are toxic molecules against neural cells. Thus, determining the generation mechanism of toxic Aβ oligomers is crucial for understanding AD pathogenesis. Aβ fibrils were reported to be disaggregated by treatment with small compounds, such as epigallocatechin gallate (EGCG) and dopamine (DA), and a loss of fibril shape and decrease in cytotoxicity were observed. However, the characteristics of intermediate products during the fibril disaggregation process are poorly understood. In this study, we found

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Fichou, Yann, Yanxian Lin, Jennifer N. Rauch, et al. "Cofactors are essential constituents of stable and seeding-active tau fibrils." Proceedings of the National Academy of Sciences 115, no. 52 (2018): 13234–39. http://dx.doi.org/10.1073/pnas.1810058115.

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Amyloid fibrils are cross-β–rich aggregates that are exceptionally stable forms of protein assembly. Accumulation of tau amyloid fibrils is involved in many neurodegenerative diseases, including Alzheimer’s disease (AD). Heparin-induced aggregates have been widely used and assumed to be a good tau amyloid fibril model for most biophysical studies. Here we show that mature fibrils made of 4R tau variants, prepared with heparin or RNA, spontaneously depolymerize and release monomers when their cofactors are removed. We demonstrate that the cross-β-sheet assembly formed in vitro with polyanion ad

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Tonniges, Jeffrey R., Benjamin Albert, Edward P. Calomeni, et al. "Collagen Fibril Ultrastructure in Mice Lacking Discoidin Domain Receptor 1." Microscopy and Microanalysis 22, no. 3 (2016): 599–611. http://dx.doi.org/10.1017/s1431927616000787.

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AbstractThe quantity and quality of collagen fibrils in the extracellular matrix (ECM) have a pivotal role in dictating biological processes. Several collagen-binding proteins (CBPs) are known to modulate collagen deposition and fibril diameter. However, limited studies exist on alterations in the fibril ultrastructure by CBPs. In this study, we elucidate how the collagen receptor, discoidin domain receptor 1 (DDR1) regulates the collagen content and ultrastructure in the adventitia of DDR1 knock-out (KO) mice. DDR1 KO mice exhibit increased collagen deposition as observed using Masson’s trich

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Song, Zhiping, Jun Zhang, and Yue Fang. "Interactions between Filament Fibrils and a Network Field." Astrophysical Journal 943, no. 2 (2023): 114. http://dx.doi.org/10.3847/1538-4357/acaefc.

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Abstract Filaments are common structures in the solar atmosphere, and usually interact with their surrounding magnetic fields. However, interactions between filaments and network fields are rare. Here, we report interactions between filament fibrils and a nearby network field in the quiet Sun by employing observations from the New Vacuum Solar Telescope (NVST) and Solar Dynamics Observatory. NVST Hα images show that several filament fibrils separated from the main body of the filament, and moved sideward. While a fibril met the network field, the movement of the fibril segment corresponding to

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Kellermayer, Miklós SZ, Ünige Murvai, Andrea Horváth, Emöke Lászlóffi, Katalin Soós та Botond Penke. "Epitaxial assembly dynamics of mutant amyloid β25–35_N27C ﬁbrils explored with time-resolved scanning force microscopy". Biophys Chem. 184C (5 вересня 2013): 54–61. https://doi.org/10.1016/j.bpc.2013.08.007.

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Amyloid β25–35 (Aβ25–35) is a toxic fragment of Alzheimer's beta peptide. We have previously shown that Aβ25–35 fibrils form a trigonally oriented network on mica by epitaxial growth mechanisms. Chemical reactivity can be furnished to the fibril by introducing a cysteine residue (Aβ25–35_N27C) while maintaining oriented assembly properties. Previously we have shown that fibril binding to mica is strongly influenced by KCl concentration. In the present work we explored the kinetics of epitaxial assembly of the mutant fibrils at different peptide a

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Birk, D. E., J. M. Fitch, J. P. Babiarz, K. J. Doane, and T. F. Linsenmayer. "Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter." Journal of Cell Science 95, no. 4 (1990): 649–57. http://dx.doi.org/10.1242/jcs.95.4.649.

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The small-diameter fibrils of the chick corneal stroma are heterotypic, composed of both collagen types I and V. This tissue has a high concentration of type V collagen relative to other type I-containing tissues with larger-diameter fibrils, suggesting that heterotypic interactions may have a regulatory role in the control of fibril diameter. The interactions of collagen types I and V were studied using an in vitro self-assembly system. Collagens were purified from lathyritic chick embryos in the presence of protease inhibitors. The type V collagen preparations contained higher molecular weig

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Li, Yan, Yang Yu та Gang Ma. "Modulation Effects of Fe3+, Zn2+, and Cu2+ Ions on the Amyloid Fibrillation of α-Synuclein: Insights from a FTIR Investigation". Molecules 27, № 23 (2022): 8383. http://dx.doi.org/10.3390/molecules27238383.

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Amyloid fibrillation of α-synuclein is implicated in the pathogenesis of Parkinson’s disease and heavy metal ions such as Fe3+, Zn2+, and Cu2+ are known to be involved in the process. In this work, we explored the use of FTIR spectroscopy to look into the modulation effects of Fe3+, Zn2+, and Cu2+ on the amyloid fibrillation of α-synuclein. We performed a curve-fitting analysis on the FTIR amide I bands of these α-synuclein fibril systems, namely, the pristine fibril and the fibrils prepared in the presence of Fe3+, Zn2+, and Cu2+. We found that the α-synuclein fibrils under the influences of

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Kadler, K. E., Y. Hojima, and D. J. Prockop. "Collagen fibrils in vitro grow from pointed tips in the C- to N-terminal direction." Biochemical Journal 268, no. 2 (1990): 339–43. http://dx.doi.org/10.1042/bj2680339.

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Growth of collagen fibrils was examined in a system in which collagen monomers are generated by specific enzymic cleavage of type IpCcollagen with procollagen C-proteinase. Fibrils formed at 37 degrees C had highly tapered and symmetrical pointed tips. The pattern of cross-striations in the pointed tips indicated that all the molecules were oriented so that the N-termini were directed towards the tip. At 29 degrees C and 32 degrees C, the fibrils formed were thicker. One end of fibrils formed at 29 degrees C was blunt, and the other was pointed. Growth of the fibrils was exclusively from point

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