Abstract
Amyloid fibril formation is a phenomenon common to many proteins and peptides. Clarifying the mechanism of amyloid fibril formation is essential not only for understanding the pathogenesis of amyloidosis but also for improving our understanding of the mechanism of protein folding. Dialysis-related amyloidosis is a common and serious complication among patients on long-term hemodialysis, in which β2-microglobulin forms amyloid fibrils. We studied the core of fibrils at single-residue resolution using recently developed H/D exchange method with the dissolution of fibrils by dimethylsulfoxide. The results suggest the mechanism of amyloid fibril formation, in which the core β-sheet formed by a minimal sequence propagates to form a rigid and extensive β-sheet network.
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