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Formation of distinct prion protein amyloid fibrils under identical experimental conditions.

ABSTRACT: Protein aggregation into amyloid fibrils is linked to multiple neurodegenerative disorders, such as Alzheimer's, Parkinson's or Creutzfeldt-Jakob disease. A better understanding of the way these aggregates form is vital for the development of drugs. A large detriment to amyloid research is the ability of amyloidogenic proteins to spontaneously aggregate into multiple structurally distinct fibrils (strains) with different stability and seeding properties. In this work we show that prion proteins are capable of forming more than one type of fibril under the exact same conditions by assessing their Thioflavin T (ThT) binding ability, morphology, secondary structure, stability and seeding potential.

SUBMITTER: Ziaunys M

PROVIDER: S-EPMC7067779 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Formation of distinct prion protein amyloid fibrils under identical experimental conditions.

Ziaunys Mantas M Sneideris Tomas T Smirnovas Vytautas V

Scientific reports 20200312 1

Protein aggregation into amyloid fibrils is linked to multiple neurodegenerative disorders, such as Alzheimer's, Parkinson's or Creutzfeldt-Jakob disease. A better understanding of the way these aggregates form is vital for the development of drugs. A large detriment to amyloid research is the ability of amyloidogenic proteins to spontaneously aggregate into multiple structurally distinct fibrils (strains) with different stability and seeding properties. In this work we show that prion proteins ...[more]

PMID: 32165692

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