Silk Reconstitution Disrupts Fibroin Self-Assembly - PubMed
- ️Thu Jan 01 2015
. 2015 Sep 14;16(9):2796-804.
doi: 10.1021/acs.biomac.5b00732. Epub 2015 Aug 18.
Affiliations
- PMID: 26284914
- DOI: 10.1021/acs.biomac.5b00732
Silk Reconstitution Disrupts Fibroin Self-Assembly
Sean R Koebley et al. Biomacromolecules. 2015.
Abstract
Using atomic force microscopy, we present the first molecular-scale comparison of two of the most important silk dopes, native (NSF) and reconstituted (RSF) silkworm fibroin. We found that both systems depended on shear to show self-assembly. Significant differences in the nature of self-assembly between NSF and RSF were shown. In the highest studied concentration of 1000 mg/L, NSF exhibited assembly into 20-30 nm-wide nanofibrils closely resembling the surface structures found in natural silk fibers. RSF, in contrast, showed no self-assembly whatsoever at the same concentration, which suggests that the reconstitution process significantly disrupts silk's inherent self-assembly capability. At lower concentrations, both RSF and NSF formed fibrils under shear, apparently denatured by the substrate. Using image analysis, we quantified the properties of these self-assembled fibrils as a function of concentration and found low-concentration fibrils of NSF to form larger continuous structures than those of RSF, further supporting NSF's superior self-assembly capabilities.
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