Effect of incubation temperature on the self-assembly of regenerated silk fibroin: A study using AFM

The distinctive mechanical and photothermal properties of Molybdenum sulfide (MoS2) have the potential for improving the functionality and utilization of silk products in various sectors. This paper reports on the preparation of regenerated silk fibroin/molybdenum disulfide (RSF/MoS2) nanoparticles hybrid fiber with different MoS2 nanoparticles contents by wet spinning. The simulated sunlight test indicated that the temperature of 2 wt% RSF/MoS2 nanoparticles hybrid fibers could rise from 20.0 °C to 81.0 °C in 1 min and 98.6 °C in 10 min, exhibiting good thermal stability. It was also demonstrated that fabrics made by manual blending portrayed excellent photothermal properties. The addition of MoS2 nanoparticles could improve the toughness of hybrid fibers, which may be since the mixing of MoS2 nanoparticles hindered the self-assembly of β-sheets in RSF solution in a concentration-dependent manner because RSF/MoS2 nanoparticles hybrid fibers showed a lower β-sheet content, crystallinity, and smaller crystallite size. This study describes a new way of producing high toughness and photothermal properties fibers for multifunctional fibers’ applications.

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Investigate the Effect of Thawing Process on the Self-Assembly of Silk Protein for Tissue Applications

BioMed Research International ◽

10.1155/2017/4263762 ◽

2017 ◽

Vol 2017 ◽

pp. 1-16 ◽

Cited By ~ 2

Author(s):

Hiep Thi Nguyen ◽

Hien Thu Luong ◽

Hai Dai Nguyen ◽

Hien Anh Tran ◽

Khon Chan Huynh ◽

...

Keyword(s):

Silk Fibroin ◽

Self Assembly ◽

Porous Scaffold ◽

Building Blocks ◽

Silk Protein ◽

The Self ◽

Porous Scaffolds ◽

Protein Chain ◽

Assembly Method ◽

Thawing Process

Biological self-assembly is a process in which building blocks autonomously organize to form stable supermolecules of higher order and complexity through domination of weak, noncovalent interactions. For silk protein, the effect of high incubating temperature on the induction of secondary structure and self-assembly was well investigated. However, the effect of freezing and thawing on silk solution has not been studied. The present work aimed to investigate a new all-aqueous process to form 3D porous silk fibroin matrices using a freezing-assisted self-assembly method. This study proposes an experimental investigation and optimization of environmental parameters for the self-assembly process such as freezing temperature, thawing process, and concentration of silk solution. The optical images demonstrated the possibility and potential of −80ST48 treatment to initialize the self-assembly of silk fibroin as well as controllably fabricate a porous scaffold. Moreover, the micrograph images illustrate the assembly of silk protein chain in 7 days under the treatment of −80ST48 process. The surface morphology characterization proved that this method could control the pore size of porous scaffolds by control of the concentration of silk solution. The animal test showed the support of silk scaffold for cell adhesion and proliferation, as well as the cell migration process in the 3D implantable scaffold.

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Influence of self-assembly regenerated silk fibroin nanofibers on the properties of electrospun materials

Bio-Medical Materials and Engineering ◽

10.3233/bme-151293 ◽

2015 ◽

Vol 26 (s1) ◽

pp. S89-S94 ◽

Cited By ~ 3

Author(s):

Huijing Zhao ◽

Xia Ren ◽

Yi Zhang ◽

Lei Huang

Keyword(s):

Silk Fibroin ◽

Self Assembly ◽

Regenerated Silk Fibroin ◽

Silk Fibroin Nanofibers

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Comparison of four synthetic model peptides to understand the role of modular motifs in the self-assembly of silk fibroin

Soft Matter ◽

10.1039/c3sm51498f ◽

2013 ◽

Vol 9 (47) ◽

pp. 11325 ◽

Cited By ~ 24

Author(s):

Mengjia Ma ◽

Jian Zhong ◽

Wenying Li ◽

Juan Zhou ◽

Zhiqiang Yan ◽

...

Keyword(s):

Silk Fibroin ◽

Self Assembly ◽

The Self ◽

Synthetic Model ◽

Model Peptides

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Surface Modification and Characterisation of Silk Fibroin Fabric Produced by the Layer-by-Layer Self-Assembly of Multilayer Alginate/Regenerated Silk Fibroin

PLoS ONE ◽

10.1371/journal.pone.0124811 ◽

2015 ◽

Vol 10 (4) ◽

pp. e0124811 ◽

Cited By ~ 19

Author(s):

Gaotian Shen ◽

Xingyou Hu ◽

Guoping Guan ◽

Lu Wang

Keyword(s):

Surface Modification ◽

Silk Fibroin ◽

Self Assembly ◽

Layer By Layer ◽

Regenerated Silk Fibroin

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The Nature of Rapidly Extracted Phycocyanin from the Blue-Green Alga Plectonema Boryanum

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100065870 ◽

1971 ◽

Vol 29 ◽

pp. 366-367

Author(s):

M. Kessel ◽

R. MacColl

Keyword(s):

Self Assembly ◽

Analytical Ultracentrifugation ◽

Uranyl Acetate ◽

The Self ◽

Major Protein ◽

Subunit Structure ◽

Blue Green Alga ◽

Thin Sections ◽

Blue Green Algae ◽

Cacodylate Buffer

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.

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