Titlebar

Export bibliographic data
Literature by the same author
plus on the publication server
plus at Google Scholar

 

Influence of repeat numbers on self-assembly rates of repetitive recombinant spider silk proteins

Title data

Humenik, Martin ; Magdeburg, Michael ; Scheibel, Thomas:
Influence of repeat numbers on self-assembly rates of repetitive recombinant spider silk proteins.
In: Journal of Structural Biology. Vol. 186 (June 2014) Issue 3 . - pp. 431-437.
ISSN 1047-8477
DOI: https://doi.org/10.1016/j.jsb.2014.03.010

Official URL: Volltext

Abstract in another language

Assembly of recombinant spider silk variants eADF4(Cn) comprising different numbers (n) of the consensus
sequence motif C, derived from the natural Araneus diadematus dragline silk ADF4, yielded indistinguishable
nanofibrils in cases of nP2. The C-module comprises 35 amino acids rich in glycine and
proline residues (in GPGXY repeats) and one polyalanine stretch (Ala)8. All variants were found to be
intrinsically disordered in solution, and upon fibril formation they converted into a cross-b structure.
Heterologous seeding indicated high structural compatibility between the different eADF4(Cn) variants,
however, their assembly kinetics differed in dependence of the number of repeats. Kinetic analysis
revealed a nucleation-growth mechanism typical for the formation of cross-b-fibrils, with nucleation
rates as well as growth rates increasing with increasing numbers of repeats. Strikingly, the single
C-module did not self-assemble into fibrils, but upon addition of heterologous seeds fibril growth could
be observed. Apparently, interconnecting of at least two C-modules significantly facilitates the structural
transformation from a disordered state into b-sheet structures, which is necessary for nucleation and
beneficial for fibril growth

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Self-assembly; Cross-b fibril; Kinetics; Polyalanine; Spider silk; Structure
Institutions of the University: 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
Research Institutions > Research Centres > Bayreuth Center for Colloids and Interfaces - BZKG
Research Institutions > Research Centres > Bayreuth Center for Molecular Biosciences - BZMB
Research Institutions > Research Centres > Research Center for Bio-Macromolecules - BIOmac
Research Institutions > Research Centres > Bayreuth Center for Material Science and Engineering - BayMAT
Faculties
Research Institutions
Research Institutions > Research Centres
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Emerging Fields > Food and Health Sciences
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Emerging Fields
Result of work at the UBT: Yes
DDC Subjects: 600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 03 Mar 2015 14:58
Last Modified: 26 Nov 2015 10:51
URI: https://eref.uni-bayreuth.de/id/eprint/7762