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Structure and pH‐induced alterations of recombinant and natural spider silk proteins in solution
Author(s) -
Leclerc Jérémie,
Lefèvre Thierry,
Pottier Fabien,
Morency LouisPhilippe,
LapointeVerreault Camille,
Gagné Stéphane M.,
Auger Michèle
Publication year - 2012
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21717
Subject(s) - chemistry , silk , spider silk , protein secondary structure , recombinant dna , dynamic light scattering , biophysics , spinning , nuclear magnetic resonance spectroscopy , glycine , chemical engineering , biochemistry , polymer chemistry , amino acid , organic chemistry , materials science , biology , nanoparticle , composite material , gene , engineering
The spinning process of spiders can modulate the mechanical properties of their silk fibers. It is therefore of primary importance to understand what are the key elements of the spider spinning process to develop efficient industrial spinning processes. We have exhaustively investigated the native conformation of major ampullate silk (MaS) proteins by comparing the content of the major ampullate gland of Nephila clavipes, solubilized MaS (SolMaS) fibers and the recombinant proteins rMaSpI and rMaSpII using 1 H solution NMR spectroscopy. The results indicate that the protein secondary structure is basically identical for the recombinant protein rMaSpI, SolMaS proteins, and the proteins in the dope, and corresponds to a disordered protein rich in 3 1 ‐helices. The data also show that glycine proton chemical shifts of rMaSpI and SolMaS are affected by pH, but that this change is not due to a modification of the secondary structure. Using a combination of NMR and dynamic light scattering, we have found that the spectral alteration of glycine is concomitant to a modification of the hydrodynamical diameter of recombinant and solubilized MaS. This led us to suggest new potential roles for the pH acidification in the spinning process of MaS proteins. © 2011 Wiley Periodicals, Inc. Biopolymers 97: 337–346, 2012.