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Relationships between physical properties and sequence in silkworm silks
- Source :
- Scientific Reports
- Publication Year :
- 2016
-
Abstract
- Silk has attracted widespread attention due to its superlative material properties and promising applications. However, the determinants behind the variations in material properties among different types of silk are not well understood. We analysed the physical properties of silk samples from a variety of silkmoth cocoons, including domesticated Bombyx mori varieties and several species from Saturniidae. Tensile deformation tests, thermal analyses and investigations on crystalline structure and orientation of the fibres were performed. The results showed that saturniid silks produce more highly-defined structural transitions compared to B. mori, as seen in the yielding and strain hardening events during tensile deformation and in the changes observed during thermal analyses. These observations were analysed in terms of the constituent fibroin sequences, which in B. mori are predicted to produce heterogeneous structures, whereas the strictly modular repeats of the saturniid sequences are hypothesized to produce structures that respond in a concerted manner. Within saturniid fibroins, thermal stability was found to correlate with the abundance of poly-alanine residues, whereas differences in fibre extensibility can be related to varying ratios of GGX motifs versus bulky hydrophobic residues in the amorphous phase.
- Subjects :
- Amino Acid Motifs
Fibroin
02 engineering and technology
010402 general chemistry
01 natural sciences
Article
Saturniidae
Bombyx mori
Tensile Strength
Ultimate tensile strength
Botany
Materials Testing
Animals
Thermal stability
Bombyx
Multidisciplinary
Birefringence
Polymer science
biology
Calorimetry, Differential Scanning
Chemistry
X-Rays
fungi
Temperature
021001 nanoscience & nanotechnology
biology.organism_classification
0104 chemical sciences
SILK
Thermogravimetry
Microscopy, Electron, Scanning
Stress, Mechanical
Deformation (engineering)
0210 nano-technology
Fibroins
Peptides
Hydrophobic and Hydrophilic Interactions
Subjects
Details
- ISSN :
- 20452322
- Volume :
- 6
- Database :
- OpenAIRE
- Journal :
- Scientific reports
- Accession number :
- edsair.doi.dedup.....4b659d0d75c51d5667deca6826fece2a