Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners.

ABSTRACT: Polyphosphates (polyPs), chains of phosphate residues found in species across nature from bacteria to mammals, were recently reported to accelerate the amyloid fibril formation of many proteins. How polyPs facilitate this process, however, remains unknown. To gain insight into their mechanisms, we used various physicochemical approaches to examine the effects of polyPs of varying chain lengths on ultrasonication-dependent α-synuclein (α-syn) amyloid formation. Although orthophosphate and diphosphate exhibited a single optimal concentration of amyloid formation, triphosphate and longer-chain phosphates exhibited two optima, with the second at a concentration lower than that of orthophosphate or diphosphate. The second optimum decreased markedly as the polyP length increased. This suggested

SUBMITTER: Yamaguchi K 

PROVIDER: S-EPMC8059054 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature