TY - JOUR

T1 - Amyloid and Amyloid-Like Aggregates

T2 - Diversity and the Term Crisis

AU - Matiiv, A. B.

AU - Trubitsina, N. P.

AU - Matveenko, A. G.

AU - Barbitoff, Y. A.

AU - Zhouravleva, G. A.

AU - Bondarev, S. A.

N1 - Funding Information: The study was funded by the Russian Foundation for Basic Research (project no. 19-14-50590). Publisher Copyright: © 2020, The Author(s). Copyright: Copyright 2020 Elsevier B.V., All rights reserved.

PY - 2020/9/1

Y1 - 2020/9/1

N2 - Active accumulation of the data on new amyloids continuing nowadays dissolves boundaries of the term "amyloid". Currently, it is most often used to designate aggregates with cross-β structure. At the same time, amyloids also exhibit a number of other unusual properties, such as: detergent and protease resistance, interaction with specific dyes, and ability to induce transition of some proteins from a soluble form to an aggregated one. The same features have been also demonstrated for the aggregates lacking cross-β structure, which are commonly called "amyloid-like" and combined into one group, although they are very diverse. We have collected and systematized information on the properties of more than two hundred known amyloids and amyloid-like proteins with emphasis on conflicting examples. In particular, a number of proteins in membraneless organelles form aggregates with cross-β structure that are morphologically indistinguishable from the other amyloids, but they can be dissolved in the presence of detergents, which is not typical for amyloids. Such paradoxes signify the need to clarify the existing definition of the term amyloid. On the other hand, the demonstrated structural diversity of the amyloid-like aggregates shows the necessity of their classification.

AB - Active accumulation of the data on new amyloids continuing nowadays dissolves boundaries of the term "amyloid". Currently, it is most often used to designate aggregates with cross-β structure. At the same time, amyloids also exhibit a number of other unusual properties, such as: detergent and protease resistance, interaction with specific dyes, and ability to induce transition of some proteins from a soluble form to an aggregated one. The same features have been also demonstrated for the aggregates lacking cross-β structure, which are commonly called "amyloid-like" and combined into one group, although they are very diverse. We have collected and systematized information on the properties of more than two hundred known amyloids and amyloid-like proteins with emphasis on conflicting examples. In particular, a number of proteins in membraneless organelles form aggregates with cross-β structure that are morphologically indistinguishable from the other amyloids, but they can be dissolved in the presence of detergents, which is not typical for amyloids. Such paradoxes signify the need to clarify the existing definition of the term amyloid. On the other hand, the demonstrated structural diversity of the amyloid-like aggregates shows the necessity of their classification.

KW - amyloid-like aggregates

KW - amyloids

KW - cross-β structure

KW - prions

KW - FIBRIL FORMATION

KW - ALZHEIMERS-DISEASE

KW - REPEAT DOMAIN

KW - FUNCTIONAL AMYLOIDS

KW - PHASE-SEPARATION

KW - TRANSCRIPTIONAL REGULATOR

KW - INTRINSICALLY DISORDERED PROTEINS

KW - cross-beta structure

KW - ANTIMICROBIAL PEPTIDE

KW - CENTRAL DOMAIN

KW - YEAST PRION

UR - http://www.scopus.com/inward/record.url?scp=85091294820&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/e09f3f29-9ee5-3543-a559-b0ffaa062825/

U2 - 10.1134/S0006297920090035

DO - 10.1134/S0006297920090035

M3 - Review article

C2 - 33050849

AN - SCOPUS:85091294820

VL - 85

SP - 1011

EP - 1034

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

SN - 0006-2979

IS - 9

ER -