Background. In β2-microglobulin-related (Aβ2M) amyloidosis, partial unfolding of β2-microglobulin (β2-m) is believed to be prerequisite to its assembly into Aβ2M amyloid fibrils in vivo. Low concentrations of sodium dodecyl sulfate induce partial unfolding of β2-m to an amyloidogenic conformer and subsequent amyloid fibril formation in vitro, but the biological molecules that induce them under ...

In the face of global warming and shrinking resources of fossil fuels the interest in solar energy has increased in recent years. However, the low energy and cost efficiency of current solar cells has up to this date hindered solar energy from playing a major role on the energy market. Photon upconversion is the process in which light of low energy is converted to high energy photons. Lately, t...

Amyloid fibrils are deposited in a number of diseases, including Alzheimer's disease, Type 2 diabetes, and the transmissible spongiform encephalopathies (TSE). These insoluble deposits are formed from normally soluble proteins that assemble to form fibrous aggregates that accumulate in the tissues. Electron microscopy has been used as a tool to examine the structure and morphology of these aggr...

Amyloid fibrils form in supersaturated solutions via a nucleation and growth mechanism. Although the structural features of amyloid fibrils have become increasingly clearer, knowledge on the thermodynamics of fibrillation is limited. Furthermore, protein aggregation is not a target of calorimetry, one of the most powerful approaches used to study proteins. Here, with β2-microglobulin, a protein...

The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative diseases. In Parkinson’s disease it is believed that the aggregation of -synuclein ( -syn) from monomers by intermediates into amyloid fibrils is the toxic diseasecausative mechanism. Here, we studied the structure of -syn in its amyloid state by using various biophysical approaches. Quenched hydrogen/...

familial amyloid polyneuropathy (fap) type iv (finnish) is a rare clinical entity with challenging neuropathy and cosmetic deficits. amyloidosis can affect peripheral sensory, motor, or autonomic nerves. nerve lesions are induced by deposits of amyloid fibrils and treatment approaches for neuropathy are challenging. involvement of cranial nerves and atrophy in facial muscles is a real concern i...

A protein, ASCA, is isolated from amyloid fibrils extracted from heart tissue of five different patients with senile cardiac amyloidosis (SCA). The proteins of all five patients showed immunological identity when reacted with an antiserum raised against one of the proteins. In contrast, no reaction was obtained with antisera against a variety of other amyloid proteins. The antiserum against the...

In murine senile amyloidosis, misfolded serum apolipoprotein (apo) A-II deposits as amyloid fibrils (AApoAII) in a process associated with aging. Mouse strains carrying type C apoA-II (APOA2C) protein exhibit a high incidence of severe systemic amyloidosis. Previously, we showed that N- and C-terminal sequences of apoA-II protein are critical for polymerization into amyloid fibrils in vitro. He...