pH-Dependent In-Cell Self-Assembly of Peptide Inhibitors Increases the Anti-Prion Activity While Decreasing the Cytotoxicity

2017 ◽  
Vol 18 (3) ◽  
pp. 943-950 ◽  
Author(s):  
Muhammad Waqas ◽  
Woo-jin Jeong ◽  
Young-Joo Lee ◽  
Dae-Hwan Kim ◽  
Chongsuk Ryou ◽  
...  
Soft Matter ◽  
2021 ◽  
Vol 17 (11) ◽  
pp. 3096-3104
Author(s):  
Valeria Castelletto ◽  
Jani Seitsonen ◽  
Janne Ruokolainen ◽  
Ian W. Hamley

A designed surfactant-like peptide is shown, using a combination of cryogenic-transmission electron microscopy and small-angle X-ray scattering, to have remarkable pH-dependent self-assembly properties.


Polyhedron ◽  
2008 ◽  
Vol 27 (12) ◽  
pp. 2672-2680 ◽  
Author(s):  
Zhao-Peng Qi ◽  
Zheng-Shuai Bai ◽  
Qing Yuan ◽  
Taka-aki Okamura ◽  
Kai Cai ◽  
...  

2019 ◽  
Vol 17 (18) ◽  
pp. 4543-4553 ◽  
Author(s):  
Jessica A. Hutchinson ◽  
Ian W. Hamley ◽  
Charlotte J. C. Edwards-Gayle ◽  
Valeria Castelletto ◽  
Cristian Piras ◽  
...  

The self-assembly of a palmitoylated peptide C16-EELNRYY based on a fragment of the gut hormone peptide PYY3–36 is investigated.


2017 ◽  
Vol 5 (16) ◽  
pp. 7555-7563 ◽  
Author(s):  
Michael C. Nolan ◽  
James J. Walsh ◽  
Laura L. E. Mears ◽  
Emily R. Draper ◽  
Matthew Wallace ◽  
...  

We show the importance of the self-assembly of a perylene bisimide on its photocatalytic activity.


Tetrahedron ◽  
2007 ◽  
Vol 63 (25) ◽  
pp. 5539-5547 ◽  
Author(s):  
Oana M. Martin ◽  
Sandro Mecozzi
Keyword(s):  

2012 ◽  
Vol 137 (19) ◽  
pp. 194902 ◽  
Author(s):  
Brian H. Morrow ◽  
Peter H. Koenig ◽  
Jana K. Shen

2015 ◽  
Vol 30 (1) ◽  
pp. 30-40 ◽  
Author(s):  
Gang Wang ◽  
Li-tao Jia ◽  
Bo Hou ◽  
De-bao Li ◽  
Jun-gang Wang ◽  
...  

Author(s):  
Sanni Voutilainen ◽  
Arja Paananen ◽  
Martina Lille ◽  
Markus Linder

<p>Protein engineering shows a wide range of possibilities for designing properties in novel materials. Following inspiration from natural systems we have studied how combinations or duplications of protein modules can be used to engineer their interactions and achieve functional properties. Here we used cellulose binding modules (CBM) coupled to spider silk N-terminal domains that dimerize in a pH-sensitive manner. We showed how the pH-sensitive switching into dimers affected cellulose binding affinity in relation to covalent coupling between CBMs. Finally, we showed how the pH-sensitive coupling could be used to assemble cellulose nanofibers in a dynamic pH-dependent way. The work shows how novel proteins can be designed by linking functional domains from widely different sources and thereby achieve new functions in the self-assembly of nanoscale materials.</p>


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