Cell-Permeable, MMP-2 Activatable, Nickel Ferrite and His-Tagged Fusion Protein Self-Assembled Fluorescent Nanoprobe for Tumor Magnetic-Targeting and Imaging

2017 ◽  
Vol 9 (45) ◽  
pp. 39209-39222 ◽  
Author(s):  
Lu Sun ◽  
Shuping Xie ◽  
Jing Qi ◽  
Ergang Liu ◽  
Di Liu ◽  
...  

2019 ◽  
Vol 2 (3) ◽  
pp. 1970005
Author(s):  
Melanie Ziegler ◽  
Xiaoqiu Xu ◽  
May Lin Yap ◽  
Houyuan Hu ◽  
Jianxiang Zhang ◽  
...  


2017 ◽  
Vol 9 (39) ◽  
pp. 34423-34434 ◽  
Author(s):  
Mario Rothbauer ◽  
Martin Frauenlob ◽  
Karoline Gutkas ◽  
Michael B. Fischer ◽  
Eva-Kathrin Sinner ◽  
...  


Author(s):  
Yang Liu ◽  
Li-Ya Niu ◽  
Yu-Zhe Chen ◽  
Qing-Zheng Yang


Nanoscale ◽  
2021 ◽  
Author(s):  
Shengsheng Cui ◽  
Shanshan Fan ◽  
Haisong Tan ◽  
Yi Lu ◽  
Yiqian Zha ◽  
...  

Near-infrared two-zone (NIR-II) fluorescence imaging has attracted attention as a non-invasive imaging technology that provides centimeter-level depth and micron-level resolution. However, producing a NIR-II fluorescent nanoprobe with uniform size, high...



2012 ◽  
Vol 78 (9) ◽  
pp. 3249-3255 ◽  
Author(s):  
Zhenlin Han ◽  
Bei Zhang ◽  
Yi E. Wang ◽  
Yi Y. Zuo ◽  
Wei Wen Su

ABSTRACTIn this study, a molecular self-assembly strategy to develop a novel protein scaffold for amplifying the extent and variety of proteins displayed on the surface ofSaccharomyces cerevisiaeis presented. The cellulosomal scaffolding protein cohesin and its upstream hydrophilic domain (HD) were genetically fused with the yeast Ure2p N-terminal fibrillogenic domain consisting of residues 1 to 80 (Ure2p1-80). The resulting Ure2p1-80-HD-cohesin fusion protein was successfully expressed inEscherichia colito produce self-assembled supramolecular nanofibrils that serve as a novel protein scaffold displaying multiple copies of functional cohesin domains. The amyloid-like property of the nanofibrils was confirmed via thioflavin T staining and atomic force microscopy. These cohesin nanofibrils attached themselves, via a green fluorescent protein (GFP)-dockerin fusion protein, to the cell surface ofS. cerevisiaeengineered to display a GFP-nanobody. The excess cohesin units on the nanofibrils provide ample sites for binding to dockerin fusion proteins, as exemplified using an mCherry-dockerin fusion protein as well as theClostridium cellulolyticumCelA endoglucanase. More than a 24-fold increase in mCherry fluorescence and an 8-fold increase in CelA activity were noted when the cohesin nanofibril scaffold-mediated yeast display was used, compared to using yeast display with GFP-cohesin that contains only a single copy of cohesin. Self-assembled supramolecular cohesin nanofibrils created by fusion with the yeast Ure2p fibrillogenic domain provide a versatile protein scaffold that expands the utility of yeast cell surface display.



2019 ◽  
Vol 2 (3) ◽  
pp. 1800133 ◽  
Author(s):  
Melanie Ziegler ◽  
Xiaoqiu Xu ◽  
May Lin Yap ◽  
Houyuan Hu ◽  
Jianxiang Zhang ◽  
...  


2015 ◽  
Vol 88 (2) ◽  
pp. 327-329 ◽  
Author(s):  
Eiji Nakata ◽  
Yoshijiro Nazumi ◽  
Yoshihiro Yukimachi ◽  
Yoshihiro Uto ◽  
Hitoshi Hori ◽  
...  


RSC Advances ◽  
2016 ◽  
Vol 6 (51) ◽  
pp. 45701-45707 ◽  
Author(s):  
Vandana Kumari ◽  
Koushik Dey ◽  
Saurav Giri ◽  
Asim Bhaumik

We report a novel approach for fabricating nanocrystalline and mesoporous nickel ferrite nanoparticles of ca. 5–9 nm size and it showed interesting memory effect as a consequence of interparticle interaction of self-assembled nanoparticles.



2018 ◽  
Vol 54 (89) ◽  
pp. 12642-12645 ◽  
Author(s):  
Pulakesh Aich ◽  
Jaeyeon An ◽  
Byeongseon Yang ◽  
Young Ho Ko ◽  
Junghyun Kim ◽  
...  

A spider with mussel: a supramolecular fiber formed by a spider dragline protein was tuned to have underwater adhesion property by genetic fusion of a mussel foot protein.





Sign in / Sign up

Export Citation Format

Share Document