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Conformational Stability and Interplay of Helical N- and C-Terminal Domains with Implications on Major Ampullate Spidroin Assembly

Title data

Bauer, Joschka ; Scheibel, Thomas:
Conformational Stability and Interplay of Helical N- and C-Terminal Domains with Implications on Major Ampullate Spidroin Assembly.
In: Biomacromolecules. (27 January 2017) .
ISSN 1526-4602
DOI: https://doi.org/10.1021/acs.biomac.6b01713

Abstract in another language

Major ampullate spidroin (MaSp) assembly starts in the abdomen of the spider, where spidroins are stored as a liquid dope at a high concentration. The dope is squeezed into the spinning duct, and assembly is finished upon drawing of fibers. Unwanted aggregation of the spidroin solution in the gland is suppressed by prestructuring of the spidroins in micelle-like assemblies, with their hydrophobic stretches being hidden from the solvent and the hydrophilic nonrepetitive amino (NRN) and carboxy (NRC) terminal domains being exposed on the micelle surface. Conversion of the fluid dope into a solid fiber is induced within the spinning duct by acidification and ion exchange (sodium chloride against potassium phosphate), with the impact on the structure of the NRN and NRC domains acting as a regulatory switch for fiber assembly. While NRN dimerizes pH-dependently in an antiparallel fashion (i.e. quaternary structural changes), the tertiary structure of dimeric NRC is changed by shear stress and a drop in pH, inducing the alignment of the intrinsically unstructured core domains accompanied by β-sheet formation of motifs of the core domain. Here, the conformational stability of NRN1 and NRC1 of Latrodectus hesperus MaSp1 were studied using independent techniques such as circular dichroism, fluorescence and absorbance spectroscopy, and scanning electron, transmission electron, and atomic force microscopy. In this context, it could be shown that strong, non-natural acidification drives NRC1 to unfold and aggregate into β-sheet-rich structures, preventing recombinant spidroins from assembling into aligned fibrils. Interestingly, NRN1 and NRC1 apparently do not interact with each other, making spidroin assembly easy to control step-by-step and straightforward due to missing unproductive side reactions.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials
Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Emerging Fields
Profile Fields > Emerging Fields > Food and Health Sciences
Research Institutions
Research Institutions > Research Centres
Research Institutions > Research Centres > Bayreuth Center for Material Science and Engineering - BayMAT
Result of work at the UBT: Yes
DDC Subjects: 600 Technology, medicine, applied sciences
600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 15 Feb 2017 07:47
Last Modified: 15 Feb 2017 07:47
URI: https://eref.uni-bayreuth.de/id/eprint/36077