Proteinase K Resistant Cores of Prions and Amyloids

Overview

Journal Prion

Specialty Biochemistry

Date 2019 Dec 27

PMID 31876447

Citations 17

Authors

Vitaly V Kushnirov

Alexander A Dergalev

Alexander I Alexandrov

Affiliations

Soon will be listed here.

Abstract

Amyloids and their infectious subset, prions, represent fibrillary aggregates with regular structure. They are formed by proteins that are soluble in their normal state. In amyloid form, all or part of the polypeptide sequence of the protein is resistant to treatment with proteinase K (PK). Amyloids can have structural variants, which can be distinguished by the patterns of their digestion by PK. In this review, we describe and compare studies of the resistant cores of various amyloids from different organisms. These data provide insight into the fine structure of amyloids and their variants as well as raise interesting questions, such as those concerning the differences between amyloids obtained and , as well as the manner in which folding of one region of the amyloid can affect other regions.

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