نتایج جستجو برای: fibril inhibitor
تعداد نتایج: 218571 فیلتر نتایج به سال:
We report here on a non-linear poroelastic model for the mechanical response of collagenous soft tissues such as articular cartilage. The tissue consists of a porous, fibril-reinforced, hyperelastic solid, saturated with an incompressible fluid, and Darcy's law governs solid-fluid interaction. The solid matrix is characterized by the isotropic hyperfoam strain energy function and its permeabili...
Since Cohen and Calkins in 1959 (6) described amyloid as composed of fibrils, there have been differing reports about the fibril width and the presence or size of l inear or globtflar subunits in the fibril. Originally, the width of the human amyloid fibril was estimated at 70 to 140 A. Later estimates of the width varied from 50 to 300 A (I, 2, 4, 5, 7, 12, 19-21, 23, 24). There have been rela...
Amyloid fibril disaggregation has been observed recently upon incubation with lipid vesicles, challenging the view of fibrils as end states of the aggregation process in vivo. Here, we follow fibril disaggregation in the presence of lipid vesicles by means of molecular dynamics simulations, using simplified models of peptides and lipids. The simulation results show that disaggregation is driven...
Windmill palm (Trachycarpus fortunei) fibre was obtained from different parts of windmill-palm trunk sheath and then treated by sodium hydroxide solution and hydrogen peroxide to obtain the treated palm fibril. The appearance of raw windmill palm fibre and treated palm fibril, morphological characteristics, and statistical analysis of fibril length, diameter, and degree of hollowness were studi...
Using replica exchange molecular dynamics simulations and an all-atom implicit solvent model, we probed the energetics of Abeta(10-40) fibril growth. The analysis of the interactions between incoming Abeta peptides and the fibril led us to two conclusions. First, considerable variations in fibril binding propensities are observed along the Abeta sequence. The peptides in the fibril and those bi...
Carnosine, a common dipeptide in mammals, has previously been shown to dissemble alpha-crystallin amyloid fibrils. To date, the dipeptide's anti-fibrillogensis effect has not been thoroughly characterized in other proteins. For a more complete understanding of carnosine's mechanism of action in amyloid fibril inhibition, we have investigated the effect of the dipeptide on lysozyme fibril format...
Mammalian tissues contain networks and ordered arrays of collagen fibrils originating from the periodic self-assembly of helical 300 nm long tropocollagen complexes. The fibril radius is typically between 25 to 250 nm, and tropocollagen at the surface appears to exhibit a characteristic twist-angle with respect to the fibril axis. Similar fibril radii and twist-angles at the surface are observe...
Extracellular polysaccharides mediate pilus retraction during social motility of Myxococcus xanthus.
Myxococcus xanthus is a Gram-negative bacterium with a complex life cycle that includes vegetative swarming and fruiting-body formation. Social (S)-motility (coordinated movement of large cell groups) requires both type IV pili and fibrils (extracellular matrix material consisting of polysaccharides and protein). Little is known about the role of this extracellular matrix, or fibril material, i...
Deciphering the links between amino acid sequence and amyloid fibril formation is key for understanding protein misfolding diseases. Here we use Monte Carlo simulations to study the aggregation of short peptides in a coarse-grained model with hydrophobic-polar (HP) amino acid sequences and correlated side chain orientations for hydrophobic contacts. A significant heterogeneity is observed in th...
A series of benzofuran derivatives have been identified as inhibitors of fibril formation in the beta-amyloid peptide. The activity of these compounds has been assessed by a novel fibril-formation-specific immunoassay and for their effects on the production of a biologically active fibril product. The inhibition afforded by the compounds seems to be associated with their binding to beta-amyloid...
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