Novel Assembly Properties of Recombinant Spider Dragline Silk Proteins

Title data

Hümmerich, Daniel ; Scheibel, Thomas ; Vollrath, Fritz ; Cohen, Shulamit ; Gat, Uri ; Ittah, Shmulik:
Novel Assembly Properties of Recombinant Spider Dragline Silk Proteins.
In: Current Biology. Vol. 14 (2004) Issue 22 . - pp. 2070-2074.
ISSN 1879-0445
DOI: https://doi.org/10.1016/j.cub.2004.11.005

Official URL:

Abstract in another language

Spider dragline silk, which exhibits extraordinary strength and toughness, is primarily composed of two related proteins that largely consist of repetitive sequences. In most spiders, the repetitive region of one of these proteins is rich in prolines, which are not present in the repetitive region of the other. The absence of prolines in one component was previously speculated to be essential for the thread structure. Here, we analyzed dragline proteins of the garden spider Araneus diadematus, ADF-3 and ADF-4, which are both proline rich, by employing the baculovirus expression system. Whereas ADF-3 represented an intrinsically soluble protein, ADF-4 was insoluble in vitro and self-assembled into filaments in the cytosol of the host insect cells. These ADF-4 filaments displayed the exceptional chemical stability of authentic silk threads. We provide evidence that the observed properties of ADF-3 and ADF-4 strongly depend on intrinsic characteristics such as hydropathicity, which differs dramatically between the two proteins, as in most other pairs of dragline silk proteins from other Araneoidea species, but not on their proline content. Our findings shed new light on the structural components of spider dragline silk, allowing further elucidation of their assembly properties, which may open the door for commercial applications.

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 > 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:	No
DDC Subjects:	600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited:	16 Mar 2015 13:05
Last Modified:	14 Feb 2023 12:09
URI:	https://eref.uni-bayreuth.de/id/eprint/8048