Electrospun scaffolds of self-assembling peptides with poly(ethylene oxide) for bone tissue engineering

2011 ◽  
Vol 7 (6) ◽  
pp. 2526-2532 ◽  
Author(s):  
Paola Brun ◽  
Francesca Ghezzo ◽  
Martina Roso ◽  
Roberta Danesin ◽  
Giorgio Palù ◽  
...  
2021 ◽  
Vol 191 ◽  
pp. 500-513
Author(s):  
Maryam Abdollahi Asl ◽  
Saeed Karbasi ◽  
Saeed Beigi-Boroujeni ◽  
Soheila Zamanlui Benisi ◽  
Mahdi Saeed

2009 ◽  
Vol 64 (1-2) ◽  
pp. 149-154 ◽  
Author(s):  
Ivo Ivanov ◽  
Ivanka Tsacheva ◽  
Vishnia Stoyanova ◽  
Miroslav Nikolov ◽  
Magdalena I. Tchorbadjieva ◽  
...  

The amphiphilic polyzwitterion (PZ) poly(ethylene oxide-b-N,N-dimethyl(methacryloyloxyethyl) ammonium propanesulfonate), zwitterionic surfactant (ZS) n-dodecyl- N,N-dimethyl-3-ammonium-1-propanesulfonate, and zwitterionic monomer (ZM) N,Ndimethyl( methacryloyloxyethyl)ammonium propanesulfonate were analyzed for their suggested chaperone-like effect on the interaction of C1q and IgG. Our results proved that the PZ retarded the C1q interaction with IgG, demonstrating a specific protein-folding helper effect. The ZS enhanced this interaction, when the ZS concentration was lower than the critical micelle concentration (CMC), and retarded it, when the ZS concentration was above the CMC. The ZM, with no self-assembling ability, did not influence this interaction. These results support the hypothesis of a hydrophobic interaction between Pts and hydrophobic domains of partly denatured protein molecules. The amphiphilic self-assemblies, formed by polyzwitterionic macromolecules or zwitterionic surfactants, have the ability to transform the hydrophobic domains of the protein molecules into hydrophilic ones, covering them with their hydrophilic parts.


2011 ◽  
Vol 95 (2) ◽  
pp. 69-80 ◽  
Author(s):  
Alberto Di Martino ◽  
Liliana Liverani ◽  
Alberto Rainer ◽  
Giuseppe Salvatore ◽  
Marcella Trombetta ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document