Controllable transition of silk fibroin nanostructures: An insight into in vitro silk self-assembly process

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


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

2017 ◽  
Vol 17 (12) ◽  
pp. 6151-6157 ◽  
Author(s):  
Xia Zhang ◽  
Ling Zhou ◽  
Chang Wang ◽  
Yang Li ◽  
Yanan Wu ◽  
...  

2015 ◽  
Vol 9 (4) ◽  
pp. 382-391 ◽  
Author(s):  
Yi Zhang ◽  
Cencen Zhang ◽  
Lijie Liu ◽  
David L. Kaplan ◽  
Hesun Zhu ◽  
...  

2015 ◽  
Vol 6 (7) ◽  
pp. 3863-3867 ◽  
Author(s):  
Takao Noguchi ◽  
Bappaditya Roy ◽  
Daisuke Yoshihara ◽  
Youichi Tsuchiya ◽  
Tatsuhiro Yamamoto ◽  
...  

A new assembly-based fluorescent sensor exhibits much improved selectivity for ATP over ADP and a broad detection range under adjusted salt conditions, providing insight into a pivotal binding mechanism in the self-assembly process.


2019 ◽  
Vol 123 (4) ◽  
pp. 2526-2532 ◽  
Author(s):  
Norma E. González-Díaz ◽  
Roberto López-Rendón ◽  
Joel Ireta

2012 ◽  
Vol 23 (20) ◽  
pp. 3936-3947 ◽  
Author(s):  
Takuya Shiota ◽  
Miyuki Maruyama ◽  
Mami Miura ◽  
Yasushi Tamura ◽  
Koji Yamano ◽  
...  

The TOM40 complex is a protein translocator in the mitochondrial outer membrane and consists of several different subunits. Among them, Tom40 is a central subunit that constitutes a protein-conducting channel by forming a β-barrel structure. To probe the nature of the assembly process of Tom40 in the outer membrane, we attached various mitochondrial presequences to Tom40 that possess sorting information for the intermembrane space (IMS), inner membrane, and matrix and would compete with the inherent Tom40 assembly process. We analyzed the mitochondrial import of those fusion proteins in vitro. Tom40 crossed the outer membrane and/or inner membrane even in the presence of various sorting signals. N-terminal anchorage of the attached presequence to the inner membrane did not prevent Tom40 from associating with the TOB/SAM complex, although it impaired its efficient release from the TOB complex in vitro but not in vivo. The IMS or matrix-targeting presequence attached to Tom40 was effective in substituting for the requirement for small Tim proteins in the IMS for the translocation of Tom40 across the outer membrane. These results provide insight into the mechanism responsible for the precise delivery of β-barrel proteins to the outer mitochondrial membrane.


2008 ◽  
pp. 1539 ◽  
Author(s):  
Scott J. Dalgarno ◽  
Nicholas P. Power ◽  
John E. Warren ◽  
Jerry L. Atwood

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