Self-assembly fabrication of microencapsulated n-octadecane with natural silk fibroin shell for thermal-regulating textiles

2016 ◽  
Vol 99 ◽  
pp. 495-501 ◽  
Author(s):  
Liang Zhao ◽  
Jie Luo ◽  
Hao Wang ◽  
Guolin Song ◽  
Guoyi Tang
2021 ◽  
Author(s):  
Kai Song ◽  
Yejing Wang ◽  
Wenjie Dong ◽  
Zhenzhen Li ◽  
Huawei He ◽  
...  

AbstractSilkworm silk is one of the best natural protein fibers spun by the silkworm at ambient temperature and pressure using aqueous silk protein solution. It is a great challenge to reproduce high-performance artificial fibers comparable to natural silk by bionics for the incomplete understanding of silkworm spinning mechanism, especially the structure and assembly of natural silk fibroin (NSF) in the silk gland. Here, we studied the structure and assembly of NSF with the assistance of amphipol and digitonin. Our results showed NSFs were present as nanofibrils primarily composed of random coils in the silk gland. Metal ions were vital for the formation of NSF nanofibrils. The successive decrease in pH from posterior silk gland (PSG) to anterior silk gland (ASG) resulted in a gradual increase in NSF hydrophobicity. NSF nanofibrils were randomly arranged from PSG to ASG-1, and then self-assembled into herringbone-like patterns near the spinneret (ASG-2) ready for silkworm spinning. Our study reveals the mechanism by which silkworms cleverly utilize metal ions and pH gradient in the silk gland to drive the programmed self-assembly of NSF from disordered nanofibrils to anisotropic liquid crystalline spinning dope (herringbone-like patterns) for silkworm spinning, thus providing novel insights into silkworm/spider spinning mechanism and bionic creation of high-performance fibers.


Biomaterials ◽  
2011 ◽  
Vol 32 (4) ◽  
pp. 1059-1067 ◽  
Author(s):  
Qiang Lu ◽  
Xiuli Wang ◽  
Shenzhou Lu ◽  
Mingzhong Li ◽  
David L. Kaplan ◽  
...  

2012 ◽  
Vol 465 ◽  
pp. 160-164 ◽  
Author(s):  
Li Mao ◽  
Yu Liu ◽  
Xi Long Wu ◽  
Shen Zhou Lu

Regenerated Antheraea Pernyi silk fibroin (ASF) solution was prepared by dissolving Antheraea Pernyi (A. pernyi) silk fiber in lithium thiocyanate solution. Atomic force microscopy (AFM) examination showed that there were many short nanofibers in regenerated ASF solution, which were made up of 10-20 nm nanospheres. In this paper, we discussed the formation mechanism of these nanofibers. The results of the surface tension showed that ASF had surface active and can significantly decline the surface tension of water from 73 mN/m to 51 mN/m. The hydrophobic side chains of ASF molecular would try to break away from water environment and thereby undergo self-assembly into nanospheres. And then, these nanospheres arrange into a short nanofiber. Then, the ASF nanofiber film was prepared by casting regenerated ASF solution blended with glycol. The structure of ASF was β-sheet and the film was water-insoluble. This blend film not only had excellent mechanical properties, but also can be biodegradated by enzyme in vitro. All of this indicated that this new regenerated ASF nanofiber film not only provided excellent biocompatibility, but also had large surface as extracellular matrix (ECM) to cell adhesion. The film made of nanofiber was similar to ECM on the nanoscale, which promoted cell migration and proliferation. In summary, it provided a great potential as a biological material.


RSC Advances ◽  
2015 ◽  
Vol 5 (81) ◽  
pp. 65684-65689 ◽  
Author(s):  
Fan Xu ◽  
Meimei Bao ◽  
Longfei Rui ◽  
Jiaojiao Liu ◽  
Jingliang Li ◽  
...  

A self-assembled lipid membrane provides a smooth, hydrophilic and biocompatible surface coating film for materials.


2020 ◽  
Vol 221 (16) ◽  
pp. 2000113 ◽  
Author(s):  
Priyanka Dubey ◽  
Sinchan Seit ◽  
Pramit K. Chowdhury ◽  
Sourabh Ghosh

2019 ◽  
Vol 89 (21-22) ◽  
pp. 4581-4594 ◽  
Author(s):  
Suhua Zhao ◽  
Hongliang Pan ◽  
Yali Liu ◽  
Yirong Zeng ◽  
Hongling Liu ◽  
...  

Historic silk fabric is an important part of Chinese precious cultural heritage and its protection has always been a major challenge. This paper proposes a bio-safety method by the chemical conjugation of transglutaminase (TGase or TG) and sodium caseinate (SC), which produced a macromolecular polymer between protein molecules and enhanced silk fabrics. The changes of the mechanical properties of the reinforced silk fabric after washing by 10 cycles were not obvious, indicating good washing durability. After TGase and SC reinforcement, the silk fibroin (SF) solution was sprayed on the surface of silk fabric to improve the mechanical properties, where the secondary structure were formed by the self-assembly of SF to improve the mechanical properties. Therefore, the breaking stress attained the maximum value when the SF solution concentration was 1.0%. Meanwhile, the breaking stress increased by about 20.89% compared with untreated silk fabric. When the artificially alkali aged silk fabric is reinforced, the breaking stress and strain of the reinforced sample increased by 37.77% relative to the alkali aged fabric. The surface morphology and secondary structure transformation of the samples were also analyzed by scanning electron microscopy and Fourier transform infrared spectroscopy, respectively. The results indicated that a significant SF layer was introduced on the surface of the silk fabric and the β-sheet structure increased due to the synergetic role of the macromolecular polymer and SF. Moreover, it is concluded that an increase in temperature and humidity will result in a decrease in the preservation index, which caused the degradation of silk fabric and proved that the preservation time of the reinforced silk fabric in the same environment was longer than that of the unreinforced sample. The biological enzyme chemical conjugation with silk fabric and physical combination of the pure SF solution is expected to be applied to the protection and enhancement of silk cultural relics.


2021 ◽  
Vol 9 (36) ◽  
pp. 12043-12048
Author(s):  
Lifeng Xu ◽  
Xiao Liang ◽  
Shuangling Zhong ◽  
Zhanfeng Li ◽  
Yan Gao ◽  
...  

2013 ◽  
Vol 9 (8) ◽  
pp. 7806-7813 ◽  
Author(s):  
S. Bai ◽  
S. Liu ◽  
C. Zhang ◽  
W. Xu ◽  
Q. Lu ◽  
...  

2015 ◽  
Vol 76 ◽  
pp. 195-202 ◽  
Author(s):  
Jian Zhong ◽  
Xunwei Liu ◽  
Daixu Wei ◽  
Juan Yan ◽  
Ping Wang ◽  
...  

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