Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson's disease.

Amyloid β-Sheet Mimics that Antagonize Amyloid Aggregation and Reduce Amyloid Toxicity

The amyloid protein aggregation associated with diseases such as Alzheimer's, Parkinson's and type II diabetes (among many others) features a bewildering variety of β-sheet-rich structures in transition from native proteins to ordered oligomers and fibres. The variation in the amino-acid sequences of the β-structures presents a challenge to developing a model system of β-sheets for the study of...

Insulin-degrading enzyme prevents α-synuclein fibril formation in a nonproteolytical manner

The insulin-degrading enzyme (IDE) degrades amyloidogenic proteins such as Amyloid β (Αβ) and Islet Amyloid Polypeptide (IAPP), i.e. peptides associated with Alzheimer's disease and type 2 diabetes, respectively. In addition to the protease activity normally associated with IDE function an additional activity involving the formation of stable, irreversible complexes with both Αβ and α-synuclein...

Photo-induced cross-linking of unmodified proteins (PICUP) applied to amyloidogenic peptides.

The assembly of amyloidogenic proteins into toxic oligomers is a seminal event in the pathogenesis of protein misfolding diseases, including Alzheimer's, Parkinson's, and Huntington's diseases, hereditary amyotrophic lateral sclerosis, and type 2 diabetes. Owing to the metastable nature of these protein assemblies, it is difficult to assess their oligomer size distribution quantitatively using ...

Association between Type-2 diabetes and Parkinson’s disease: a cross-talk between amylin and α-synuclein

Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy

Aggregation of misfolded proteins or peptides is a common feature of neurodegenerative diseases including Alzheimer's, Parkinson's, Huntington's, prion and other diseases. Recent years have witnessed a growing number of reports of overlap in neuropathological features that were once thought to be unique to only one neurodegenerative disorder. However, the origin for the overlap remains unclear....