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Mussel collagen molecules with silk-like domains as load-bearing elements in distal byssal threads

Title data

Hagenau, Anja ; Papadopoulos, Periklis ; Kremer, Friedrich ; Scheibel, Thomas:
Mussel collagen molecules with silk-like domains as load-bearing elements in distal byssal threads.
In: Journal of Structural Biology. Vol. 175 (September 2011) Issue 3 . - pp. 339-347.
ISSN 1047-8477
DOI: https://doi.org/10.1016/j.jsb.2011.05.016

Official URL: Volltext

Abstract in another language

Mechanically stressed biological materials like tendon, spider silk or mussel byssal threads are typically composite materials comprising multi-domain proteins, in which molecular building blocks contribute to overall material function.

Mussel byssal threads are the anchorage of sessile mytilid mussels, which withstand recurring external loads from waves and tides. A single thread is elastic and ductile proximally, while the distal portion exhibits an extraordinary stiffness and toughness with a transient gradient of both mechanical features along the thread. The main components of byssal threads include a set of various collagen-like structural proteins (preCols) consisting of a collagenous core sequence flanked by globular domains. Here, structural analysis using polarized Fourier-transform infrared spectroscopy (FTIR) on stretched distal portions of mussel byssal threads determines the impact of external linear load on various molecular moieties. It is concluded that the preCol collagenous core domain is the main load-bearing element in distal byssal threads, while polyalanine beta-sheets in the flanking domains, similar to those found in spider silk proteins, provide high stiffness at low strains. Load dissipation is mediated by domain stretching of amorphous glycine-rich helical moieties followed by complete unfolding of the preCol flanking domains.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Biopolymers; PreCols; Spider silk; Infrared spectroscopy; Force measurements; Protein fibers
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 > 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: 01 Jul 2015 10:08
Last Modified: 26 Nov 2015 10:51
URI: https://eref.uni-bayreuth.de/id/eprint/15615