Search results for "amyloids"

Designing trehalose-conjugated peptides for the inhibition of Alzheimer’s Aβ oligomerization and neurotoxicity

2008

Highly tunable protein microspheres for drug delivery

2019

It is well-known that protein amyloid aggregation has profound implications in several neurodegenerative diseases. In contrast, a natural role for amyloid structures as protection, adhesion and storage materials in living system is also reported, promoting protein aggregates as an interesting platform for the design of multifunctional biomaterials. Among the broad range of different amyloid structures protein particulates deserve special attention; they are spherical protein aggregates with radius ranging from hundreds of nm to few um which are readily formed in solution at pHs values near the isoelectric point of the protein they are made of. Interestingly, particulate appears to be a gene…

Concanavalin A aggregation and toxicity on cell cultures

2009

A number of neurodegenerative diseases are known to involve protein aggregation. Common mechanisms and structural properties of amyloids are thought to be involved in aggregation-related cytotoxicity. In this context we propose an experimental study on Concanavalin A (Con A) aggregation and use it as a model to study the relationship between cell toxicity and aggregation processes. Depending on solution conditions, Con A aggregation has been monitored by static and dynamic light scattering, Thioflavin T emission, and FTIR absorption. The morphology of different aggregate species was verified by means of Atomic Force Microscopy and Confocal Microscopy. During the aggregation pathway the nati…

Copper(ii) and zinc(ii) dependent effects on Aβ42 aggregation: a CD, Th-T and SFM study

2013

A? aggregation is a central event in Alzheimer's disease (AD). In vitro evidence indicates that A? aggregation and fibrillogenesis are significantly influenced by the employed experimental conditions. Indeed, although it is widely established that metal ions, such as copper and zinc, have significant effects on the A? aggregation process, their actual role in A? fibrillogenesis is still debated. In this work the effects of a molar excess of zinc(ii) and/or copper(ii) ions on the A?42 aggregation process and the morphology of the resultant aggregates have been compared in samples exhibiting different initial conformations. CD spectroscopy, Th-T-induced fluorescence and Scanning Force Microsc…

Formation of covalent di-tyrosine dimers in recombinant α-synuclein

2015

Parkinson's disease is associated with fibril deposition in the diseased brain. Misfolding events of the intrinsically disordered synaptic protein α-synuclein are suggested to lead to the formation of transient oligomeric and cytotoxic species. The etiology of Parkinson's disease is further associated with mitochondrial dysfunction and formation of reactive oxygen species. Oxidative stress causes chemical modification of native α-synuclein, plausibly further influencing misfolding events. Here, we present evidence for the spontaneous formation of covalent di-tyrosine α-synuclein dimers in standard recombinant protein preparations, induced without extrinsic oxidative or nitrative agents. The…

THz spectroscopy study of amyloid fibrils

2013

In suitable conditions proteins can modify their native conformation and associate to form aggregates with different morphologies in dependence on the external physico-chemical conditions. This phenomenon, one of the most challenging in life sciences, is associated with widely diffused pathologies such as Alzheimer’s, Parkinson’s and Creutzfeldt-Jacob’s diseases. Of particular relevance are ordered elongated aggregates with highly organized patterns of hydrogen-bonds, known as amyloid fibrils. While much biological and structural information are available about amyloids, and in spite of the fundamental paradigm of structure-dynamics-function relation in proteins, much less is known about th…