Using a simple in vitro amyloidopathy CAD neuronal model, infrared (IR) 1068 nm light treatment (5 x 3 minutes) was investigated as a novel neuroprotection strategy. Synthetic human β-amyloid(1-42) peptide was subjected to aggregation in a test-tube, and shown to form fibrils of a range of sizes (individually ~10 μm), which compromised the cellular nuclear integrity of CAD cells in culture, and...

Objective(s): Neuroprotective effect of creatine (Cr) against β-amyloid (Aβ) is reported in an in vitro study. This study investigated the effect of Cr supplementation on β-amyloid toxicity in vivo. Materials and Methods: Thirty two, male Wistar rats were divided into 4 groups. During ten weeks of study, control group went through no surgical or dietary intervention. At the 4th week of study S...

Insight into how amyloid β (Aβ) aggregation occurs in vivo is vital for understanding the molecular pathways that underlie Alzheimer's disease and requires new techniques that provide detailed kinetic and mechanistic information. Using noninvasive fluorescence lifetime recordings, we imaged the formation of Aβ(1-40) and Aβ(1-42) aggregates in live cells. For both peptides, the cellular uptake v...

The deposition of insoluble amyloid fibrils resulting from the aggregation of the human islet amyloid polypeptide (hIAPP) within the islet of Langerhans is a pathological feature of type 2 diabetes mellitus (T2DM). Increasing evidence indicates that biological membranes play a key role in amyloid aggregation, modulating among others the kinetics of amyloid formation, and being the target of tox...

Abnormal aggregation of amyloid-β is a very complex and heterogeneous process. Owing to methodological limitations, the pathway still not fully understood. Herein new approach presented in which secondary structure single aggregates investigated with tip-enhanced Raman spectroscopy (TERS) liquid environment. Clearly resolved TERS signatures amide I III bands enabled detailed analysis molecular ...

Aggregation of amyloid-β (Aβ) peptide, a 39- to 43-residue fragment of the amyloid precursor protein, is associated with Alzheimer's disease, the most common form of dementia in the elderly population. Several experimental studies have tried to characterize the atomic details of amyloid fibrils, which are the final product of Aβ aggregation. Much less is known about species forming during the e...

Many amyloid proteins misfold into β-sheet aggregates upon interacting with biomembranes at the onset of diseases, such as Parkinson's disease and type II diabetes. The molecular mechanisms triggering aggregation depend on the orientation of β-sheets at the cell membranes. However, understanding how β-sheets adsorb onto lipid/aqueous interfaces is challenging. Here, we combine chiral sum freque...

objective(s): neuroprotective effect of creatine (cr) against β-amyloid (aβ) is reported in an in vitro study. this study investigated the effect of cr supplementation on β-amyloid toxicity in vivo. materials and methods: thirty two, male wistar rats were divided into 4 groups. during ten weeks of study, control group went through no surgical or dietary intervention. at the 4th week of study sh...

Amyloid fibrils and amorphous aggregates are two types of aberrant aggregates associated with protein misfolding diseases. Although they differ in morphology, the two forms are often treated indiscriminately. β(2)-microglobulin (β2m), a protein responsible for dialysis-related amyloidosis, forms amyloid fibrils or amorphous aggregates depending on the NaCl concentration at pH 2.5. We compared t...

Alzheimer's disease (AD) is a progressive neurodegenerative disease characterized by the accumulation and aggregation of extracellular amyloid β (Aβ) peptides and intracellular aggregation of hyper-phosphorylated tau protein. Recent evidence indicates that accumulation and aggregation of intracellular amyloid β peptides may also play a role in disease pathogenesis. This would suggest that intra...