Current Protein and Peptide Science - Volume 11, Issue 5, 2010

The growing interest in membrane interactions of amyloidogenic peptides and proteins emanates from the realization that lipids and membranes play important, potentially central, roles in the toxicity and pathological pathways of amyloid diseases. Expanding body of evidence indicates that lipid binding of amyloidogenic peptides, and amyloid peptide association with cellular membranes are critical to the onset and progressi Read More

Gradual changes in steady-state levels of beta amyloid peptides (Aβ) in the brain are considered as initial step in the amyloid cascade hypothesis of Alzheimer's disease (AD). Aβ is a product of the secretase cleavage of the amyloid precursor protein and there is evidence that the membrane lipid environment may modulate secretase activity and alters its function. Aβ disturbs membrane properties of artificial and isolated biologic Read More

Prion diseases are a class of fatal neurodegenerative disorders that affect mammals and are characterized by their unique transmissibility and the nature of the infectious agent. When the physiological prion protein (PrPC) becomes corrupted (PrPSc) it accumulates in the brain, promoting infection and self-propagation via recruitment of PrPC. Although with identical sequence, PrPC and PrPSc differ in their physicochemical Read More

α-Synuclein is a small neuronal protein that has been implicated to play an important role in Parkinson's disease. Genetic mutations and multiplications in the α-synuclein gene can cause familial forms of the disease. In aggregated fibrillar form, α-synuclein is the main component of Lewy bodies, the intraneuronal inclusion bodies characteristic of Parkinson's disease. The loss of functional dopaminergic neurons in Par Read More

The past fifteen years have led to a profound re-consideration of the molecular and cellular basis of amyloid diseases. Since the formulation of the amyloid hypothesis in 1991-1992, increasing interest was initially focused at amyloid fibrils and, subsequently, at their precursors, oligomers and pre-fibrillar aggregates as main culprits of cell impairment and demise, particularly in neurodegenerative diseases with amyloid depositi Read More

Attempts to understand the biophysical foundations and biochemical consequences of protein aggregation process are greatly aided by conditions which provide either robust and reliable reaction conditions or constitute mimics of the physiological conditions. While both anionic surfactants such as SDS and fluorinated alcohols such as TFE are often championed as membrane mimics in one way or another, it is probably fair to say Read More

The growing interest in membrane interactions of amyloidogenic peptides and proteins emanates from the realization that lipids and membranes play important, potentially central, roles in the toxicity and pathological pathways of amyloid diseases. Expanding body of evidence indicates that lipid binding of amyloidogenic peptides and amyloid peptide association with cellular membranes is critical in the onset and progression Read More

The famous Kramers rate theory for diffusion-controlled reactions has been extended in numerous ways and successfully applied to many types of reactions. Its application to protein folding reactions has been of particular interest in recent years, as many researchers have performed experiments and simulations to test whether folding reactions are diffusion- controlled, whether the solvent is the source of the reaction Read More