The critical role of water in spider silk and its consequence for protein mechanics

C. P. Brown, J. MacLeod, H. Amenitsch, F. Cacho-Nerin, H. S. Gill, A. J. Price, E. Traversa, S. Licoccia, F. Rosei

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Due to its remarkable mechanical and biological properties, there is considerable interest in understanding, and replicating, spider silk's stress-processing mechanisms and structure-function relationships. Here, we investigate the role of water in the nanoscale mechanics of the different regions in the spider silk fibre, and their relative contributions to stress processing. We propose that the inner core region, rich in spidroin II, retains water due to its inherent disorder, thereby providing a mechanism to dissipate energy as it breaks a sacrificial amide-water bond and gains order under strain, forming a stronger amide-amide bond. The spidroin I-rich outer core is more ordered under ambient conditions and is inherently stiffer and stronger, yet does not on its own provide high toughness. The markedly different interactions of the two proteins with water, and their distribution across the fibre, produce a stiffness differential and provide a balance between stiffness, strength and toughness under ambient conditions. Under wet conditions, this balance is destroyed as the stiff outer core material reverts to the behaviour of the inner core.
Original languageEnglish
Pages (from-to)3805-3811
Number of pages7
JournalNanoscale
Volume3
Issue number9
DOIs
Publication statusPublished - Sep 2011

Fingerprint

Silk
Mechanics
Amides
Proteins
Water
Toughness
Stiffness
Fibers
Processing

Cite this

Brown, C. P., MacLeod, J., Amenitsch, H., Cacho-Nerin, F., Gill, H. S., Price, A. J., ... Rosei, F. (2011). The critical role of water in spider silk and its consequence for protein mechanics. Nanoscale, 3(9), 3805-3811. https://doi.org/10.1039/C1NR10502G

The critical role of water in spider silk and its consequence for protein mechanics. / Brown, C. P.; MacLeod, J.; Amenitsch, H.; Cacho-Nerin, F.; Gill, H. S.; Price, A. J.; Traversa, E.; Licoccia, S.; Rosei, F.

In: Nanoscale, Vol. 3, No. 9, 09.2011, p. 3805-3811.

Research output: Contribution to journalArticle

Brown, CP, MacLeod, J, Amenitsch, H, Cacho-Nerin, F, Gill, HS, Price, AJ, Traversa, E, Licoccia, S & Rosei, F 2011, 'The critical role of water in spider silk and its consequence for protein mechanics', Nanoscale, vol. 3, no. 9, pp. 3805-3811. https://doi.org/10.1039/C1NR10502G
Brown CP, MacLeod J, Amenitsch H, Cacho-Nerin F, Gill HS, Price AJ et al. The critical role of water in spider silk and its consequence for protein mechanics. Nanoscale. 2011 Sep;3(9):3805-3811. https://doi.org/10.1039/C1NR10502G
Brown, C. P. ; MacLeod, J. ; Amenitsch, H. ; Cacho-Nerin, F. ; Gill, H. S. ; Price, A. J. ; Traversa, E. ; Licoccia, S. ; Rosei, F. / The critical role of water in spider silk and its consequence for protein mechanics. In: Nanoscale. 2011 ; Vol. 3, No. 9. pp. 3805-3811.
@article{3621164976da476881b9f4f803eec4ab,
title = "The critical role of water in spider silk and its consequence for protein mechanics",
abstract = "Due to its remarkable mechanical and biological properties, there is considerable interest in understanding, and replicating, spider silk's stress-processing mechanisms and structure-function relationships. Here, we investigate the role of water in the nanoscale mechanics of the different regions in the spider silk fibre, and their relative contributions to stress processing. We propose that the inner core region, rich in spidroin II, retains water due to its inherent disorder, thereby providing a mechanism to dissipate energy as it breaks a sacrificial amide-water bond and gains order under strain, forming a stronger amide-amide bond. The spidroin I-rich outer core is more ordered under ambient conditions and is inherently stiffer and stronger, yet does not on its own provide high toughness. The markedly different interactions of the two proteins with water, and their distribution across the fibre, produce a stiffness differential and provide a balance between stiffness, strength and toughness under ambient conditions. Under wet conditions, this balance is destroyed as the stiff outer core material reverts to the behaviour of the inner core.",
author = "Brown, {C. P.} and J. MacLeod and H. Amenitsch and F. Cacho-Nerin and Gill, {H. S.} and Price, {A. J.} and E. Traversa and S. Licoccia and F. Rosei",
year = "2011",
month = "9",
doi = "10.1039/C1NR10502G",
language = "English",
volume = "3",
pages = "3805--3811",
journal = "Nanoscale",
issn = "2040-3364",
publisher = "Royal Society of Chemistry",
number = "9",

}

TY - JOUR

T1 - The critical role of water in spider silk and its consequence for protein mechanics

AU - Brown, C. P.

AU - MacLeod, J.

AU - Amenitsch, H.

AU - Cacho-Nerin, F.

AU - Gill, H. S.

AU - Price, A. J.

AU - Traversa, E.

AU - Licoccia, S.

AU - Rosei, F.

PY - 2011/9

Y1 - 2011/9

N2 - Due to its remarkable mechanical and biological properties, there is considerable interest in understanding, and replicating, spider silk's stress-processing mechanisms and structure-function relationships. Here, we investigate the role of water in the nanoscale mechanics of the different regions in the spider silk fibre, and their relative contributions to stress processing. We propose that the inner core region, rich in spidroin II, retains water due to its inherent disorder, thereby providing a mechanism to dissipate energy as it breaks a sacrificial amide-water bond and gains order under strain, forming a stronger amide-amide bond. The spidroin I-rich outer core is more ordered under ambient conditions and is inherently stiffer and stronger, yet does not on its own provide high toughness. The markedly different interactions of the two proteins with water, and their distribution across the fibre, produce a stiffness differential and provide a balance between stiffness, strength and toughness under ambient conditions. Under wet conditions, this balance is destroyed as the stiff outer core material reverts to the behaviour of the inner core.

AB - Due to its remarkable mechanical and biological properties, there is considerable interest in understanding, and replicating, spider silk's stress-processing mechanisms and structure-function relationships. Here, we investigate the role of water in the nanoscale mechanics of the different regions in the spider silk fibre, and their relative contributions to stress processing. We propose that the inner core region, rich in spidroin II, retains water due to its inherent disorder, thereby providing a mechanism to dissipate energy as it breaks a sacrificial amide-water bond and gains order under strain, forming a stronger amide-amide bond. The spidroin I-rich outer core is more ordered under ambient conditions and is inherently stiffer and stronger, yet does not on its own provide high toughness. The markedly different interactions of the two proteins with water, and their distribution across the fibre, produce a stiffness differential and provide a balance between stiffness, strength and toughness under ambient conditions. Under wet conditions, this balance is destroyed as the stiff outer core material reverts to the behaviour of the inner core.

UR - http://www.scopus.com/inward/record.url?scp=80052565827&partnerID=8YFLogxK

UR - http://dx.doi.org/10.1039/C1NR10502G

U2 - 10.1039/C1NR10502G

DO - 10.1039/C1NR10502G

M3 - Article

VL - 3

SP - 3805

EP - 3811

JO - Nanoscale

JF - Nanoscale

SN - 2040-3364

IS - 9

ER -