Search results for " Fibrils"
showing 10 items of 14 documents
Trifluoroethanol modulates α-synuclein amyloid-like aggregate formation, stability and dissolution
2016
The conversion of proteins into amyloid fibrils and other amyloid-like aggregates is closely connected to the onset of a series of age-related pathologies. Upon changes in environmental conditions, amyloid-like aggregates may also undergo disassembly into oligomeric aggregates, the latter being recognized as key effectors in toxicity. This indicates new possible routes for in vivo accumulation of toxic species. In the light of the recognized implication of α-Synuclein (αSN) in Parkinson's disease, we present an experimental study on supramolecular assembly of αSN with a focus on stability and disassembly paths of such supramolecular aggregate species. Using spectroscopic techniques, two-pho…
Nucleation mechanisms and morphologies in insulin amyloid fibril formation
2011
Amyloid Fibrils Formation of Concanavalin A at Basic pH
2011
Mechanisms of partial unfolding and aggregation of proteins are of extreme interest in view of the fact that several human pathologies are characterized by the formation and deposition of protein-insoluble material, mainly composed of amyloid fibrils. Here we report on an experimental study on the heat-induced aggregation mechanisms, at basic pH, of concanavalin A (ConA), used as a model system. Thioflavin T (ThT) fluorescence and multiangle light scattering allowed us to detect different intertwined steps in the formation of ConA aggregates. In particular, the ThT fluorescence increase, observed in the first phase of aggregation, reveals the formation of intermolecular β-sheet structure wh…
Detection of Type VII collagen in odontogenic keratocyst: An immunohistochemical study
2019
Background Separation of the epithelial lining from the underlying connective tissue wall has been a frequently observed and unique feature in odontogenic keratocysts (OKC), but not in other odontogenic cysts nor neoplasms. No study on OKC has been reported evaluating the role of type VII Collagen, the anchoring fibrils, which function in stabilising the epithelial structure. The purpose of this study was to assess the role of type VII collagen in the fragility of the epithelium leading to a high recurrence rate in OKCs. Material and Methods Immunohistochemical staining with Abcam® Monoclonal Mouse Anti-Collagen VII Antibody [LH7.2] (used at a dilution of 1:200) on 30 tissues of OKC. The ch…
THERMALLY INDUCED FIBRILLAR AGGREGATION OF BOVINE SERUM ALBUMIN
2008
Phasor-FLIM analysis of Thioflavin T self-quenching in Concanavalin amyloid fibrils
2020
The formation of amyloid structures has traditionally been related to human neurodegenerative pathologies and, in recent years, the interest in these highly stable nanostructures was extended to biomaterial sciences. A common method to monitor amyloid growth is the analysis of Thioflavin T fluorescence. The use of this highly selective dye, diffused worldwide, allows mechanistic studies of supramolecular assemblies also giving back important insight on the structure of these aggregates. Here we present experimental evidence of self-quenching effect of Thioflavin T in presence of amyloid fibrils. A significant reduction of fluorescence lifetime of this dye which is not related to the propert…
Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq
2015
Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to…
Self-Organization Pathways and Spatial Heterogeneity in Insulin Amyloid Fibril Formation
2009
At high temperature and low pH, the protein hormone insulin is highly prone to form amyloid fibrils, and for this reason it is widely used as a model system to study fibril formation mechanisms. In this work, we focused on insulin aggregation mechanisms occurring in HCl solutions (pH 1.6) at 60 degrees C. By means of in situ Thioflavin T (ThT) staining, the kinetics profiles were characterized as a function of the protein concentration, and two concurrent aggregation pathways were pointed out, being concentration dependent. In correspondence to these pathways, different morphologies of self-assembled protein molecules were detected by atomic force microscopy images also evidencing the prese…
In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
2019
Hfq is a bacterial protein that regulates gene expression at the post-transcriptional level in Gram-negative bacteria. We have previously shown that Escherichia coli Hfq protein, and more precisely its C-terminal region (CTR), self-assembles into an amyloid-like structure in vitro. In the present work, we present evidence that Hfq unambiguously forms amyloid structures also in vivo. Taking into account the role of this protein in bacterial adaptation and virulence, our work opens possibilities to target Hfq amyloid self-assembly and cell location, with potential to block bacterial adaptation and treat infections. Fil: Partouche, David. Centre National de la Recherche Scientifique; Francia. …