Amyloid fibrils are β-sheet rich protein aggregates that are strongly associated with various neurodegenerative diseases. Raman spectroscopy has been broadly utilized to investigate protein aggregation and amyloid fibril formation and has been shown to be capable of revealing changes in secondary and tertiary structures at all stages of fibrillation. When coupled with atomic force (AFM) and sca...

The amyloid hypothesis causatively relates the fibrillar deposits of amyloid β peptide (Aβ) to Alzheimer's disease (AD). More recent data, however, identify the soluble oligomers as the major cytotoxic entities. Pyroglutamylated Aβ (pE-Aβ) is present in AD brains and exerts augmented neurotoxicity, which is believed to result from its higher β-sheet propensity and faster fibrillization. While t...

Alzheimer's disease (AD) is a form of dementia and the most common progressive neurodegenerative disease (ND). The targeting of amyloid-beta (Aβ) aggregation is one of the most widely used strategies to manage AD, and efforts are being made globally to develop peptide-based compounds for the early diagnosis and treatment of AD. Here, we briefly discuss the use of peptide-based compounds for the...

Mammalian small heat-shock proteins (sHSPs) are molecular chaperones that form polydisperse and dynamic complexes with target proteins, serving as a first line of defense in preventing their aggregation into either amorphous deposits or amyloid fibrils. Their apparently broad target specificity makes sHSPs attractive for investigating ways to tackle disorders of protein aggregation. The two mos...

We present a study of the dynamics of protein aggregation using a common path heterodyne Bloch surface wave sensing scheme. We demonstrate the ability to detect, during thermal incubation, the early events linked to the aggregation of proteins related to conformational diseases. Alzheimer's amyloid-β 1-42 is used to demonstrate the efficiency of the method. A model based on elementary interacti...

The 16–22 amino acid fragment of the β-amyloid peptide associated with the Alzheimer’s disease, Aβ, is capable of forming amyloid fibrils. Here we study the aggregation mechanism of Aβ16−22 peptides by unbiased thermodynamic simulations at the atomic level for systems of one, three and six Aβ16−22 peptides. We find that the isolated Aβ16−22 peptide is mainly a random coil in the sense that both...

Alzheimer’s disease (AD) is the most common cause of late life dementia. Substantial clinical and experimental evidence supports the hypothesis that amyloid β-protein (Aβ) aggregation produces assemblies with potent neurotoxic properties that cause AD. For this reason, it is important to elucidate the structural dynamics of Aβ aggregation at atomic level. We apply the discrete molecular dynamic...

Bovine β-lactoglobulin (β-lg), consisting of pronounced β-sheet content, have been chosen as a model protein which on prolonged thermal treatment forms large molecular aggregates similar to Alzheimer’s type amyloid fibrils. The effects of L-arginine (free base) in thermal aggregation process of β-lg were monitored at varying concentrations. Concentration dependent opposite behaviour has been re...

The 16–22 amino acid fragment of the β-amyloid peptide associated with the Alzheimer’s disease, Aβ, is capable of forming amyloid fibrils. Here we study the aggregation mechanism of Aβ16−22 peptides by unbiased thermodynamic simulations at the atomic level for systems of one, three and six Aβ16−22 peptides. We find that the isolated Aβ16−22 peptide is mainly a random coil in the sense that both...