Silk Fiber Assembly Studied by Synchrotron Radiation SAXS/WAXS and Raman Spectroscopy
Citations Over TimeTop 10% of 2008 papers
Abstract
We have characterized the steps involved in silk assembly from the protein solution into beta-type fibers by a combination of small-angle and wide-angle X-ray scattering and Raman spectroscopy. The aggregation process was studied in a concentric flow microfluidic cell, which allows mimicking the spinning duct. The fibroin molecule in solution shows an elongated shape with a maximum diameter of 38 nm. During the pH-driven initial assembly step, large-scale aggregates of fibroin molecules with a maximum diameter of about 260 nm are formed. Raman spectroscopy on the dried, fibrous material shows a principally alpha-helical silk I secondary structure, which is transformed gradually into beta-type silk II by increasing immersion times in water. The formation of crystalline beta-sheet domains within the fiber is confirmed by wide-angle X-ray scattering. The assembly process resembles the peptide condensation-ordering model proposed for amyloid cross-beta formation.
Related Papers
- → Raman spectroscopic characterization of Bombyx mori silk fibroin: Raman spectrum of Silk I(2001)156 cited
- → Tuning the structure and performance of silk biomaterials by combining mulberry and non-mulberry silk fibroin(2017)37 cited
- → Design, Expression and Solid-State NMR Characterization of Silk-Like Materials Constructed from Sequences of Spider Silk, Samia cynthia ricini and Bombyx mori Silk Fibroins(2005)31 cited
- → Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: A platform for the production of tuneable material(2014)9 cited
- Biological and physical aspects(2000)