BACKGROUND Beside neurofibrillary tangles, amyloid plaques are the major histological hallmarks of Alzheimer's disease (AD) being composed of aggregated fibrils of β-amyloid (Aβ). During the underlying fibrillogenic pathway, starting from a surplus of soluble Aβ and leading to mature fibrils, multiple conformations of this peptide appear, including oligomers of various shapes and sizes. To furt...

The inverse sequences of naturally occurring proteins display different folding and structural properties fail to retain the functions native despite identical fundamental features, such as amino acid composition, hydrophobicity, etc. To gain insight into physical mechanisms underlying secondary structure formation aggregation direct retro amyloidogenic peptides, we probed fibrillogenesis accom...

The peptide Boc-Val-Phe-OMe 1 bearing sequence similarity with the central hydrophobic cluster (CHC) of Alzheimer's Aβ(18-19) peptide self-assembles to produce amyloid-like straight unbranched fibrils as examined by atomic force microscopy and Congo red assay. Single crystal X-ray diffraction offers the atomic level structure of the supramolecular parallel β-sheet aggregation and antiparallel s...

Background: The British Precursor Protein (BRI2) influences Amyloid Precursor Protein metabolism. Results: BRI2 lowers β-amyloid peptide levels by increasing levels of secreted insulin degrading enzyme (IDE) in both cells and mice. Conclusion: BRI2 as a receptor protein regulates IDE levels and in turn promotes βamyloid degradation. Significance: Targeting the regulation of IDE may lead to new ...

Alzheimer's disease is the most common form of senile dementia in world, and amyloid β peptide1-42 (Aβ1-42) one its two principal biological hallmarks. While interactome concept was getting forward scientific community, we proposed that study molecular interactions peptide with membranes will allow to highlight underlying mechanisms responsive AD. We have developed simple liposomal formulations...

We have previously reported that pyrroloquinoline quinone (PQQ) prevents the amyloid formation of α-synuclein, amyloid β(1-42) (Aβ(1-42)), and mouse prion protein. Moreover, PQQ-modified α-synuclein and a proteolytic fragment of the PQQ-modified α-synuclein are able to inhibit the amyloid formation of α-synuclein. Here, we identified the peptide sequences that play an important role as PQQ-mod...