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Mechanisms of amyloid fibril formation – focus on domain‐swapping
Author(s) -
Žerovnik Eva,
Stoka Veronika,
Mirtič Andreja,
Gunčar Gregor,
Grdadolnik Jože,
Staniforth Rosemary A.,
Turk Dušan,
Turk Vito
Publication year - 2011
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2011.08149.x
Subject(s) - fibril , amyloid (mycology) , amyloid fibril , biophysics , protein aggregation , chemistry , protein folding , domain (mathematical analysis) , computational biology , amyloid β , biochemistry , biology , disease , medicine , inorganic chemistry , mathematical analysis , mathematics , pathology
Conformational diseases constitute a group of heterologous disorders in which a constituent host protein undergoes changes in conformation, leading to aggregation and deposition. To understand the molecular mechanisms of the process of amyloid fibril formation, numerous in vitro and in vivo studies, including model and pathologically relevant proteins, have been performed. Understanding the molecular details of these processes is of major importance to understand neurodegenerative diseases and could contribute to more effective therapies. Many models have been proposed to describe the mechanism by which proteins undergo ordered aggregation into amyloid fibrils. We classify these as: (a) templating and nucleation; (b) linear, colloid‐like assembly of spherical oligomers; and (c) domain‐swapping. In this review, we stress the role of domain‐swapping and discuss the role of proline switches.