Hierarchical spidroin micellar nanoparticles as the fundamental precursors of spider silks
Abstract
The true physical form of the proteins within the silk glands of spiders that permits storage at very high concentrations rather than as precipitated material prior to being transformed into solid silk fibers remains one of the fundamental mysteries that has limited our ability to produce artificial silks of the quality of natural silks. Here we determine that spider silk proteins are stored as complex micellar nanoparticles composed of assembled subdomains. When extruded during the silk spinning process, these subdomains undergo fibrillization while remaining assembled in micelles. Knowledge of the nanostructured protein assemblies in the dope is critical to the basic understanding of the spinning process and to our ability to mimic the natural material properties in synthetic analogues.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Oct 22, 2018
- Source ID
- 10.1073/pnas.1810203115
Entities
People
- Brian R. Cherry
- Christopher J. Forman
- David Onofrei
- Dian Xu
- Dillan Stengel
- Gregory P. Holland
- J. Bennett Addison
- Jeffery L Yarger
- John D. Roehling
- Lucas R Parent
- Nathan C. Gianneschi
- Samrat A. Amin
Organizations
- Arizona State University
- Army Research Office
- Lawrence Livermore National Laboratory
- National Institutes of Health
- National Science Foundation
- Northwestern University
- San Diego State University
- United States Department of Defense
- United States Department of Energy