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Int. J. Mol. Sci. 2016, 17(8), 1353; doi:10.3390/ijms17081353

Major Ampullate Spider Silk with Indistinguishable Spidroin Dope Conformations Leads to Different Fiber Molecular Structures

Regroupement québécois de Recherche sur la Fonction, l'Ingénierie et les Applications des Protéines (PROTEO), Centre de Recherche sur les Matériaux Avancés (CERMA), Centre Québécois sur les Matériaux Fonctionnels (CQMF), Département de Chimie, Université Laval, Pavillon Alexandre-Vachon, Ville de Québec, QC G1V 0A6, Canada
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Academic Editors: John G. Hardy and Chris Holland
Received: 21 July 2016 / Revised: 11 August 2016 / Accepted: 15 August 2016 / Published: 18 August 2016
(This article belongs to the Special Issue Silk-Based Materials: From Production to Characterization)
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Abstract

To plentifully benefit from its properties (mechanical, optical, biological) and its potential to manufacture green materials, the structure of spider silk has to be known accurately. To this aim, the major ampullate (MA) silk of Araneus diadematus (AD) and Nephila clavipes (NC) has been compared quantitatively in the liquid and fiber states using Raman spectromicroscopy. The data show that the spidroin conformations of the two dopes are indistinguishable despite their specific amino acid composition. This result suggests that GlyGlyX and GlyProGlyXX amino acid motifs (X = Leu, Glu, Tyr, Ser, etc.) are conformationally equivalent due to the chain flexibility in the aqueous environment. Species-related sequence specificity is expressed more extensively in the fiber: the β-sheet content is lower and width of the orientation distribution of the carbonyl groups is broader for AD (29% and 58°, respectively) as compared to NC (37% and 51°, respectively). β-Sheet content values are close to the proportion of polyalanine segments, suggesting that β-sheet formation is mainly dictated by the spidroin sequence. The extent of molecular alignment seems to be related to the presence of proline (Pro) that may decrease conformational flexibility and inhibit chain extension and alignment upon drawing. It appears that besides the presence of Pro, secondary structure and molecular orientation contribute to the different mechanical properties of MA threads. View Full-Text
Keywords: Raman spectromicroscopy; spider silk fibers; spinning dope; silk protein structure; molecular orientation; orientation distribution function Raman spectromicroscopy; spider silk fibers; spinning dope; silk protein structure; molecular orientation; orientation distribution function
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Dionne, J.; Lefèvre, T.; Auger, M. Major Ampullate Spider Silk with Indistinguishable Spidroin Dope Conformations Leads to Different Fiber Molecular Structures. Int. J. Mol. Sci. 2016, 17, 1353.

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