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Global analysis of kinetics reveals the role of secondary nucleation in recombinant spider silk self-assembly

DOI zum Zitieren der Version auf EPub Bayreuth: https://doi.org/10.15495/EPub_UBT_00007225
URN to cite this document: urn:nbn:de:bvb:703-epub-7225-7

Title data

Hovanová, Veronika ; Hovan, Andrej ; Žoldák, Gabriel ; Sedlák, Erik ; Humenik, Martin:
Global analysis of kinetics reveals the role of secondary nucleation in recombinant spider silk self-assembly.
In: Protein Science. Vol. 32 (2023) Issue 8 . - e4722.
ISSN 1469-896X
DOI der Verlagsversion: https://doi.org/10.1002/pro.4722

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Project information

Project financing: Deutscher Akademischer Austauschdienst

Abstract

Abstract Recombinant spider silk proteins can be prepared in scalable fermentation processes and have been proven as sources of biomaterials for biomedical and technical applications. Nanofibrils, formed through the self-assembly of these proteins, possess unique structural and mechanical properties, serving as fundamental building blocks for the fabrication of micro- and nanostructured scaffolds. Despite significant progress in utilizing nanofibrils-based morphologies of recombinant spider silk proteins, a comprehensive understanding of the molecular mechanisms of nanofibrils self-assembly remains a challenge. Here, a detailed kinetic study of nanofibril formation from a recombinant spider silk protein eADF4(C16) in dependence on the protein concentration, seeding, and temperature is provided. For the global fitting of kinetic data obtained during the fibril formation, we utilized the online platform AmyloFit. Evaluation of the data revealed that the self-assembly mechanism of recombinant spider silk is dominated by secondary nucleation. Thermodynamic analyses show that both primary and secondary nucleations, as well as the elongation step of the eADF4(C16), are endothermic processes.

Further data

Item Type: Article in a journal
Keywords: fibrils; recombinant protein; secondary nucleation; self-assembly; spider silk
DDC Subjects: 600 Technology, medicine, applied sciences > 620 Engineering
Institutions of the University: Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials
Language: English
Originates at UBT: Yes
URN: urn:nbn:de:bvb:703-epub-7225-7
Date Deposited: 13 Oct 2023 07:28
Last Modified: 13 Oct 2023 09:07
URI: https://epub.uni-bayreuth.de/id/eprint/7225

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