NDLI: Nanostructure and molecular mechanics of spider dragline silk protein assemblies

Content Provider	PubMed Central
Author	Sinan, Keten Buehler, Markus J.
Copyright Year	2010
Abstract	Spider silk is a self-assembling biopolymer that outperforms most known materials in terms of its mechanical performance, despite its underlying weak chemical bonding based on H-bonds. While experimental studies have shown that the molecular structure of silk proteins has a direct influence on the stiffness, toughness and failure strength of silk, no molecular-level analysis of the nanostructure and associated mechanical properties of silk assemblies have been reported. Here, we report atomic-level structures of MaSp1 and MaSp2 proteins from the Nephila clavipes spider dragline silk sequence, obtained using replica exchange molecular dynamics, and subject these structures to mechanical loading for a detailed nanomechanical analysis. The structural analysis reveals that poly-alanine regions in silk predominantly form distinct and orderly beta-sheet crystal domains, while disorderly regions are formed by glycine-rich repeats that consist of 31-helix type structures and beta-turns. Our structural predictions are validated against experimental data based on dihedral angle pair calculations presented in Ramachandran plots, alpha-carbon atomic distances, as well as secondary structure content. Mechanical shearing simulations on selected structures illustrate that the nanoscale behaviour of silk protein assemblies is controlled by the distinctly different secondary structure content and hydrogen bonding in the crystalline and semi-amorphous regions. Both structural and mechanical characterization results show excellent agreement with available experimental evidence. Our findings set the stage for extensive atomistic investigations of silk, which may contribute towards an improved understanding of the source of the strength and toughness of this biological superfibre.
Related Links	http://dx.doi.org/10.1098/rsif.2010.0149
Ending Page	1721
Page Count	13
Starting Page	1709
File Format	PDF
ISSN	17425689
e-ISSN	17425662
Journal	Journal of the Royal Society Interface
Issue Number	53
Volume Number	7
Language	English
Publisher	The Royal Society
Publisher Date	2010-12-06
Access Restriction	Open
Rights Holder	The Royal Society
Subject Keyword	Biotechnology Biophysics Biochemistry Bioengineering Biomaterials Biomedical Engineering Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry Biomaterials Biophysics Bioengineering Biomedical Engineering Biotechnology

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