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The relevance of silks to amyloids

Dicko, Cedric LU orcid ; Porter, David and Vollrath, Fritz (2010) p.51-70
Abstract
At the heart of protein's aggregation are specific molecular events; and how they are modulated by changes in solvent conditions and temperature is key to our understanding and control of aggregation. A certain class of structural fibrous proteins may provide the answer. Indeed, spider silk and silkworm silk proteins have evolved to readily form ‘insoluble’ ordered structures. But, to date little is known about the series of association steps involved in the nucleation and growth of silk aggregates. Here we review silk β-fold propensity from an evolutionary and modelisation point of view, to provide a number of key features shared with amyloids (as well as prions). These results could form the basis for novel analytical comparative studies... (More)
At the heart of protein's aggregation are specific molecular events; and how they are modulated by changes in solvent conditions and temperature is key to our understanding and control of aggregation. A certain class of structural fibrous proteins may provide the answer. Indeed, spider silk and silkworm silk proteins have evolved to readily form ‘insoluble’ ordered structures. But, to date little is known about the series of association steps involved in the nucleation and growth of silk aggregates. Here we review silk β-fold propensity from an evolutionary and modelisation point of view, to provide a number of key features shared with amyloids (as well as prions). These results could form the basis for novel analytical comparative studies within fibre-forming proteins research. (Less)
Please use this url to cite or link to this publication:
author
; and
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
host publication
Functional Amyloid Aggregation
editor
Riggaci, Stefania and Bucciantini, Monica
pages
20 pages
publisher
Research Signpost
ISBN
978-81-308-0425-5
language
English
LU publication?
no
id
7c4bcaaa-f0a8-44c6-92a0-6b23685048c1
date added to LUP
2020-06-11 10:35:35
date last changed
2021-04-08 09:11:13
@inbook{7c4bcaaa-f0a8-44c6-92a0-6b23685048c1,
  abstract     = {{At the heart of protein's aggregation are specific molecular events; and how they are modulated by changes in solvent conditions and temperature is key to our understanding and control of aggregation. A certain class of structural fibrous proteins may provide the answer. Indeed, spider silk and silkworm silk proteins have evolved to readily form ‘insoluble’ ordered structures. But, to date little is known about the series of association steps involved in the nucleation and growth of silk aggregates. Here we review silk β-fold propensity from an evolutionary and modelisation point of view, to provide a number of key features shared with amyloids (as well as prions). These results could form the basis for novel analytical comparative studies within fibre-forming proteins research.}},
  author       = {{Dicko, Cedric and Porter, David and Vollrath, Fritz}},
  booktitle    = {{Functional Amyloid Aggregation}},
  editor       = {{Riggaci, Stefania and Bucciantini, Monica}},
  isbn         = {{978-81-308-0425-5}},
  language     = {{eng}},
  pages        = {{51--70}},
  publisher    = {{Research Signpost}},
  title        = {{The relevance of silks to amyloids}},
  year         = {{2010}},
}