Polyphosphates diminish solubility of a globular protein and thereby promote amyloid aggregation.

ABSTRACT: Structural changes of globular proteins and their resultant amyloid aggregation have been associated with various human diseases, such as lysozyme amyloidosis and light-chain amyloidosis. Because many globular proteins can convert into amyloid fibrils in vitro, the mechanisms of amyloid fibril formation have been studied in various experimental systems, but several questions remain unresolved. Here, using several approaches, such as turbidimetry, fluorescence and CD spectroscopy, EM, and isothermal titration calorimetry, we examined the binding of polyphosphates to hen egg-white lysozyme under acidic conditions and observed polyphosphate-induced structural changes of the protein promoting its aggregation. Our data indicate that negatively charged polyphosphates bind to protein molec

SUBMITTER: Sasahara K 

PROVIDER: S-EPMC6802520 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature