Environment-Induced Silk Fibroin Conformation Based on the Magnetic Resonance Spectroscopy

Jiang, Teng; Zhou, Ping

doi:10.5772/18479

Cited by 5 publications

(8 citation statements)

References 36 publications

(45 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…26 In this study, we aimed to understand the mechanism of the structural changes due to the hydrophilic-lipophilic environment. Studying the environment effects on the silk broin conformation will help to elucidate the mechanism of silk spinning.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

The influence of the hydrophilic–lipophilic environment on the structure of silk fibroin protein

Zhang

et al. 2015

J. Mater. Chem. B

View full text Add to dashboard Cite

The present study examines the influence of the hydrophilic-lipophilic environment, mediated by small molecules, on the structural changes in silk protein fibroin. Small molecules mediate the various hydrophilic-lipophilic balances (HLBs) that impact the organisation of silk protein chains. Changes in the silk fibroin structure due to additives are related to the HLB value. At HLB > 10, silk fibroin primarily forms Silk I crystalline structures. Small molecules with HLB < 8.9 primarily induce the formation of Silk II crystalline structures. When 8.9 < HLB < 10, the crystalline structure of silk is related to the content of small molecules. The Silk I structure is primarily formed when the content of small molecules is low, whereas the Silk II structure is formed when the small molecule content is high. The structure of silk fibroin is maintained by regulating the HLB in the fibroin environment. This type of control for the functional design of materials may play a role in fine-tuning the biomaterial properties of silk fibroin protein.

show abstract

Section: Discussionmentioning

confidence: 99%

“…The environment of silk spinning, including the shearing strength, pH, concentration of metal ions, concentration of the silk broins and types of metal ions, was investigated. 26 In this study, we aimed to understand the mechanism of the structural changes due to the hydrophilic-lipophilic environment.…”

Section: Discussionmentioning

confidence: 99%

The influence of the hydrophilic–lipophilic environment on the structure of silk fibroin protein

Zhang

et al. 2015

J. Mater. Chem. B

View full text Add to dashboard Cite

show abstract

“…Therefore, understanding the relationships between the secondary structures of silk fibroin-based biomaterials and cellular behavior is important for the development of silk fibroin-based biomaterials. Previous studies have reported that random coils and silk I structures are transformed into silk II structures by external stimuli, such as temperature (Hu et al, 2011;Tretinnikov & Tamada, 2001), pH (Zhou et al, 2004;Matsumoto et al, 2006), ions (Jiang & Zhou, 2011) and organic solvents (Jeong et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

The influence of thermal treatments on the secondary structure of silk fibroin scaffolds and their interaction with fibroblasts

Hashimoto

Nakamura

Tamada

et al. 2020

PeerJ Materials Science

View full text Add to dashboard Cite

Background Recently, silk fibroin-based biomaterials have received attention for application in tissue engineering and drug delivery systems. The usefulness of heat sterilization methods for silk fibroin-based biomaterials was investigated in this study as all biomaterials are required to undergo a sterilization process when they are used in medical devices. Methods The influence of wet and dry heating on the properties of fibroin molecules in silk fibroin sponges was investigated by measurements of solid-state 13C cross-polarization/magic angle spinning (CP/MAS) nuclear magnetic resonance (NMR) spectroscopy, thermogravimetric analyses, strength tests, and cell proliferation/migration assays. Results 13C CP/MAS NMR spectra of wet-heated sponges revealed no changes in the molecular structure below 50 °C. However, above 60 °C, the crystalline structure of the silk proteins transitioned from silk I to silk II; the silk II:silk I ratio increased with temperature. In contrast, dry heating (below 190 °C for up to 180 min) induced no structural changes in the fibroin molecules. These results indicate that, although autoclave sterilization (121 °C for 20 min) induces structural changes in silk fibroin sponges, no such changes are observed with the dry-heat sterilization (180 °C for 30 min). Sterilized sponges with a silk I structure can be obtained using dry-heat method during sterilization. Moreover, the structural differences between the wet- and dry-heated silk fibroin sponges did not influence their interaction with fibroblasts. Discussion This study indicates that both autoclaving and dry heating are acceptable sterilization methods for silk fibroin-based sponges as the scaffold. In particular, dry heating maintains the stability of the secondary structure of the sterilized silk fibroin-based biomaterials.

show abstract

“…Fibril formation can be studied by the methods of fluorescence in thioflavin T upon protein bonding [21], UV-vis absorption of congo red upon binding into protein [22][23], scanning electron microscopy (SEM) [24], transmission electron microscopy (TEM) [25], atomic force microscopy (AFM) [9,26], cryoelectron microscopy [27], Fourier-transform infrared spectroscopy (FTIR) [28], X-ray diffraction (XRD) [29] and solid state nuclear magnetic resonance (NMR) [30].…”

mentioning

confidence: 99%

“…Fibroin constitutes a light-chain, a heavy-chain and a sub-chain, and 85% of the molecular weight of this protein results from the heavy chain. Fibroin heavy chain contains 5263 amino acids mainly including glycine, alanine and serine [30]. Fibroin has applications in oxygen-and vapor-permeable films, enzyme immobilization, tissue engineering, artificial ligament production and drug delivery with a high adaptability with mammals' cells [41].…”

mentioning

confidence: 99%

Study of Nanofibrils Formation of Fibroin Protein in Specific Thermal and Acidity Conditions

2020

View full text Add to dashboard Cite

Background: Amyloid fibrils are insoluble arranged aggregates of proteins that are fibrillar in structure and related to many diseases (at least 20 types of illnesses) and also create many pathologic conditions. Therefore understanding the circumstance of fibril formation is very important. Objectives: This study aims to work on fibrillar structure formation of fibroin (as a model protein). Material and Methods: In this experimental study, fibroin was extracted from bombyx mori silk cocoon, and the concentration was obtained by Bradford method. The protein was incubated in a wide range of times (0 min to 7 days) in specific acidity and thermal conditions (pH=1.6, T=70 °C). The assays of UV-vis spectroscopy with congo red, field emission scanning electron microscopy, transmission electron microscopy, atomic force microscopy and circular dichroism spectroscopy were employed to monitor the fibrillation process. Results: Fibroin assemblies were formed upon the process of aggregation and fibril formation with a variety of morphology ranging from nanoparticles to elongated fibrils. Conclusion: The results showed progressive pathway of fibril formation.

show abstract

Environment-Induced Silk Fibroin Conformation Based on the Magnetic Resonance Spectroscopy

Cited by 5 publications

References 36 publications

The influence of the hydrophilic–lipophilic environment on the structure of silk fibroin protein

The influence of the hydrophilic–lipophilic environment on the structure of silk fibroin protein

The influence of thermal treatments on the secondary structure of silk fibroin scaffolds and their interaction with fibroblasts

Study of Nanofibrils Formation of Fibroin Protein in Specific Thermal and Acidity Conditions

Contact Info

Product

Resources

About