Search results for "fibrillogenesis"

Experimental Inhibition of Fibrillogenesis and Neurotoxicity by amyloid-beta (Aβ) and Other Disease-Related Peptides/Proteins by Plant Extracts and H…

2012

Amyloid-β (Aβ) fibrillogenesis and associated cyto/neurotoxicity are major pathological events and hallmarks in diseases such as Alzheimer’s disease (AD). The understanding of Aβ molecular pathogenesis is currently a pharmacological target for rational drug design and discovery based on reduction of Aβ generation, inhibition of Aβ fibrillogenesis and aggregation, enhancement of Aβ clearance and amelioration of associated cytotoxicity. Molecular mechanisms for other amyloidoses, such as transthyretin amyloidosis, AL-amyloidosis, as well as α-synuclein and prion protein are also pharmacological targets for current drug therapy, design and discovery. We report on natural herbal compounds and e…

Thioflavin T Promotes Aβ(1−40) Amyloid Fibrils Formation

2015

Fibrillogenesis of the small peptide Aβ(1-40) is considered to be the hallmark of Alzheimer's disease. Some evidence indicates small oligomers, rather than mature fibrils, as the key cytotoxic agents. The fluorescent dye Thioflavin T (ThT) is often used to detect amyloid deposits in both in vivo and in vitro experiments, and it is used to study kinetic measurements, under the fundamental hypothesis that this probe does not influence the aggregation processes. We report experimental data showing that ThT may promote the Aβ(1-40) peptide amyloid aggregation changing solvent-peptide interactions and stabilizing more ordered β-like conformation. This finding has a two-fold importance: It is a f…

Entrapment of Aβ(1-40) peptide in unstructured aggregates

2012

Recognizing the complexity of the fibrillogenesis process provides a solid ground for the development of therapeutic strategies aimed at preventing or inhibiting protein-protein aggregation. Under this perspective, it is meaningful to identify the possible aggregation pathways and their relative products. We found that Aβ-peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid β-conformation. ThT binding kinetics was used to monitor aggregate formation. Circular dichroism spectroscopy, AFM imaging, static and dynamic light scattering were used for structural and morphological characterization of the aggre…

Fibrillogenesis of Hen Egg-White Lysozyme at acid pH

2009

Role of repulsive interaction on the fibrillogenesis of hen egg-white lysozyme

2010

Fibrillogenesis of hen egg-white lysozyme at acidic pH

2009

Role of electrostatic interactions in the fibrillogenesis of lysozyme

2011

Integrin-mediated Cell Adhesion to Type I Collagen Fibrils

2004

In the integrin family, the collagen receptors form a structurally and functionally distinct subgroup. Two members of this subgroup, α1β1 and α2β1 integrins, are known to bind to monomeric form of type I collagen. However, in tissues type I collagen monomers are organized into large fibrils immediately after they are released from cells. Here, we studied collagen fibril recognition by integrins. By an immunoelectron microscopy method we showed that integrin α2I domain is able to bind to classical D-banded type I collagen fibrils. However, according to the solid phase binding assay, the collagen fibril formation appeared to reduce integrin α1I and α2I domain avidity to collagen and to lower …