![]() These include the well-known neurological disorders such as Alzheimer’s, Parkinson’s disease and amyotrophic lateral sclerosis (ALS), but also a range of systemic or localised amyloid disorders that affect organs including the heart, kidney, pancreas, kidney and others (for a review see 4). The deposition of amyloid fibrils is associated with an array of usually untreatable human diseases that are collectively known as amyloidoses. Beyond this ordered core, disordered regions likely help define the fibril’s interactome and biological activity in vivo 3. All amyloid fibrils have a common ordered core involving β-strands that are stacked parallel to the fibril axis and separated by ~4.8 Å 1, 2. ![]() Self-assembly of peptides or proteins into amyloid fibrils is a complex process in which a protein precursor rearranges its initial structure and oligomerises to form elongated, unbranched fibrils with a cross-β fold. ![]()
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