Impact of calcium chloride concentration on structure and thermal property of Thai silk fibroin films

Wang, Fang; Yu, Haiyang; Gu, Zhenggui; Si, Lina; Liu, Qichun; Hu, Xiao

doi:10.1007/s10973-017-6388-z

Cited by 21 publications

(41 citation statements)

References 28 publications

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“…While the CRS and TRS samples in our study were grown in different regions (China and Thailand) and have different thermal properties [ 28 , 29 , 30 ], where they all came from Bombyx Mori silkworm species. Therefore, we considered that these two kinds of silk have the same cohesive energy E coh and degree of freedom N.…”

Section: Resultsmentioning

confidence: 99%

“…In the glass transition region, when the semi-crystalline polymer material changes from the solid state to the flowing liquid state, the specific heat of the semi-crystalline polymer material undergoes a discontinuous mutation during the heating process [ 28 , 29 ]. Our previous studies on silk fibroin films by scanning electron microscopy (SEM) [ 30 ] and X-ray diffraction (XRD) [ 33 ] showed that a high CaCl 2 concentration can significantly reduce the silk fibril structure and micro-/nanoscale morphology in the silk film. Further, two small diffraction peaks appeared at 20.7° and 24.0° in the XRD curves of low CaCl 2 concentration sample (e.g., TSF-1.5), which is recognized as the silk I structure.…”

Section: Resultsmentioning

confidence: 99%

“…Various silkworm leaves or foods may lead to differences in their cocoons, such as the color and strength. In our previous work, Indian Antheraea mylitta , Philosamia ricini , Antheraea assamensis , Thailand and Chinese Bombyx mori mulberry ( Thai , Chin ) silk films have been successfully regenerated from the aqueous solution [ 30 ]. Moreover, it was found that Chin and Thai silk fibroin films can be regenerated through a calcium chloride-formic acid (CaCl 2 /FA) solution system [ 31 ].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Exploring the Structural Transformation Mechanism of Chinese and Thailand Silk Fibroin Fibers and Formic-Acid Fabricated Silk Films

Liu

Fang

et al. 2018

IJMS

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Silk fibroin (SF) is a protein polymer derived from insects, which has unique mechanical properties and tunable biodegradation rate due to its variable structures. Here, the variability of structural, thermal, and mechanical properties of two domesticated silk films (Chinese and Thailand B. Mori) regenerated from formic acid solution, as well as their original fibers, were compared and investigated using dynamic mechanical analysis (DMA) and Fourier transform infrared spectrometry (FTIR). Four relaxation events appeared clearly during the temperature region of 25 °C to 280 °C in DMA curves, and their disorder degree (fdis) and glass transition temperature (Tg) were predicted using Group Interaction Modeling (GIM). Compared with Thai (Thailand) regenerated silks, Chin (Chinese) silks possess a lower Tg, higher fdis, and better elasticity and mechanical strength. As the calcium chloride content in the initial processing solvent increases (1%–6%), the Tg of the final SF samples gradually decrease, while their fdis increase. Besides, SF with more non-crystalline structures shows high plasticity. Two α- relaxations in the glass transition region of tan δ curve were identified due to the structural transition of silk protein. These findings provide a new perspective for the design of advanced protein biomaterials with different secondary structures, and facilitate a comprehensive understanding of the structure-property relationship of various biopolymers in the future.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Exploring the Structural Transformation Mechanism of Chinese and Thailand Silk Fibroin Fibers and Formic-Acid Fabricated Silk Films

Liu

Fang

et al. 2018

IJMS

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“…An isoelectric point (IEP) below pH 7 and molecular weight of 83 kDa have been reported for regenerated silk fibroin, but the latter value may vary depending on the extraction procedure and duration of treatment [ 22 , 23 ]. The repetition of amino acids in the pattern (Gly-Ser-Gly-Ala-Gly-Ala) n leads to crystalline beta-sheets that are then stacked in an antiparallel configuration [ 24 , 25 , 26 ]. This structure gives silk fibroin robust mechanical properties and high tensile strength.…”

Section: Categories Of Protein Materialsmentioning

confidence: 99%

Protein Polymer-Based Nanoparticles: Fabrication and Medical Applications

DeFrates

Markiewicz

Gallo

et al. 2018

IJMS

Self Cite

168

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Nanoparticles are particles that range in size from about 1–1000 nanometers in diameter, about one thousand times smaller than the average cell in a human body. Their small size, flexible fabrication, and high surface-area-to-volume ratio make them ideal systems for drug delivery. Nanoparticles can be made from a variety of materials including metals, polysaccharides, and proteins. Biological protein-based nanoparticles such as silk, keratin, collagen, elastin, corn zein, and soy protein-based nanoparticles are advantageous in having biodegradability, bioavailability, and relatively low cost. Many protein nanoparticles are easy to process and can be modified to achieve desired specifications such as size, morphology, and weight. Protein nanoparticles are used in a variety of settings and are replacing many materials that are not biocompatible and have a negative impact on the environment. Here we attempt to review the literature pertaining to protein-based nanoparticles with a focus on their application in drug delivery and biomedical fields. Additional detail on governing nanoparticle parameters, specific protein nanoparticle applications, and fabrication methods are also provided.

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“…Silks have been subjected to calorimetric tests for over 20 years but with the focus either on natural spun fibers (which are not directly relevant in the context of this work) or artificial silk feedstocks/films, where processing has altered the state of hydration so much that these artificial silks may no longer represent a native unspun silk protein/model aquamelt . However, in the early 2000s, Tanaka et al.…”

Section: Introductionmentioning

confidence: 99%

Differential Scanning Calorimetry of Native Silk Feedstock

Holland

Hawkins²,

Frydrych³

et al. 2018

Macromolecular Bioscience

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Native silk proteins, extracted directly from the silk gland prior to spinning, offer access to a naturally hydrated protein that has undergone little to no processing. Combined with differential scanning calorimetry (DSC), it is possible to probe the thermal stability and hydration status of silk and thus investigate its denaturation and solidification, echoing that of the natural spinning process. It is found that native silk is stable between −10 °C and 55 °C, and both the high‐temperature enthalpy of denaturation (measured via modulated temperature DSC) and a newly reported low‐temperature ice‐melting transition may serve as useful quality indicators in the future for artificial silks. Finally, compared to albumin, silk's denaturation enthalpy is much lower than expected, which is interpreted within a recently proposed entropic desolvation framework which can serve to unveil the low‐energy aquamelt processing pathway.

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Impact of calcium chloride concentration on structure and thermal property of Thai silk fibroin films

Cited by 21 publications

References 28 publications

Exploring the Structural Transformation Mechanism of Chinese and Thailand Silk Fibroin Fibers and Formic-Acid Fabricated Silk Films

Exploring the Structural Transformation Mechanism of Chinese and Thailand Silk Fibroin Fibers and Formic-Acid Fabricated Silk Films

Protein Polymer-Based Nanoparticles: Fabrication and Medical Applications

Differential Scanning Calorimetry of Native Silk Feedstock

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