The role of salt and shear on the storage and assembly of spider silk proteins

Lukas Eisoldt; John G. Hardy; Markus Heim; Thomas R. Scheibel

doi:10.1016/j.jsb.2009.12.027

The role of salt and shear on the storage and assembly of spider silk proteins

Lukas Eisoldt, John G. Hardy, Markus Heim, Thomas R. Scheibel^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

62 Citations (Scopus)

624 Downloads (Pure)

Abstract

Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of beta-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structure-function relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo. (C) 2009 Elsevier Inc. All rights reserved.

Original language	English
Pages (from-to)	413-419
Number of pages	7
Journal	Journal of structural biology
Volume	170
Issue number	2
Early online date	04 Jan 2010
DOIs	https://doi.org/10.1016/j.jsb.2009.12.027
Publication status	Published - May 2010

Keywords

Spider silk
Protein assembly
Salt
Shear
MAJOR AMPULLATE GLAND
C-TERMINAL DOMAIN
FIBER FORMATION
HOFMEISTER SERIES
DRAGLINE
CONFORMATION
ORIENTATION
MECHANISM
INSECTS
FIBROIN

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Biomaterials

Access to Document

10.1016/j.jsb.2009.12.027

The role of salt and shear on the storage and assembly of spider silk proteins
NOTICE: this is the author’s version of a work that was accepted for publication in Journal of Structural Biology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Structural Biology, [VOL170, ISSUE2, (May, 2010)] DOI: 10.1016/j.jsb.2009.12.027
Accepted author manuscript, 375 KB
supplementary information
NOTICE: this is the author’s version of a work that was accepted for publication in Journal of Structural Biology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Structural Biology, [VOL170, ISSUE2, (May, 2010)] DOI: 10.1016/j.jsb.2009.12.027
Accepted author manuscript, 64.9 KB

http://www.sciencedirect.com/science/article/pii/S1047847709003542

Cite this

@article{c7bc03c93dce4791a2c1112b102f14db,

title = "The role of salt and shear on the storage and assembly of spider silk proteins",

abstract = "Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of beta-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structure-function relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo. (C) 2009 Elsevier Inc. All rights reserved.",

keywords = "Spider silk, Protein assembly, Salt, Shear, MAJOR AMPULLATE GLAND, C-TERMINAL DOMAIN, FIBER FORMATION, HOFMEISTER SERIES, DRAGLINE, CONFORMATION, ORIENTATION, MECHANISM, INSECTS, FIBROIN",

author = "Lukas Eisoldt and Hardy, {John G.} and Markus Heim and Scheibel, {Thomas R.}",

year = "2010",

month = may,

doi = "10.1016/j.jsb.2009.12.027",

language = "English",

volume = "170",

pages = "413--419",

journal = "Journal of structural biology",

issn = "1047-8477",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - The role of salt and shear on the storage and assembly of spider silk proteins

AU - Eisoldt, Lukas

AU - Hardy, John G.

AU - Heim, Markus

AU - Scheibel, Thomas R.

PY - 2010/5

Y1 - 2010/5

N2 - Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of beta-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structure-function relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo. (C) 2009 Elsevier Inc. All rights reserved.

AB - Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of beta-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structure-function relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo. (C) 2009 Elsevier Inc. All rights reserved.

KW - Spider silk

KW - Protein assembly

KW - Salt

KW - Shear

KW - MAJOR AMPULLATE GLAND

KW - C-TERMINAL DOMAIN

KW - FIBER FORMATION

KW - HOFMEISTER SERIES

KW - DRAGLINE

KW - CONFORMATION

KW - ORIENTATION

KW - MECHANISM

KW - INSECTS

KW - FIBROIN

U2 - 10.1016/j.jsb.2009.12.027

DO - 10.1016/j.jsb.2009.12.027

M3 - Article

VL - 170

SP - 413

EP - 419

JO - Journal of structural biology

JF - Journal of structural biology

SN - 1047-8477

IS - 2

ER -

The role of salt and shear on the storage and assembly of spider silk proteins

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Fingerprint

Cite this