PEG coated vesicles from mixtures of Pluronic P123 and l-α-phosphatidylcholine: structure, rheology and curcumin encapsulation

2017 ◽  
Vol 19 (39) ◽  
pp. 26821-26832 ◽  
Author(s):  
Bijaideep Dutta ◽  
K. C. Barick ◽  
Gunjan Verma ◽  
V. K. Aswal ◽  
Inbar Freilich ◽  
...  

PEGylated vesicles from co-assembly of block copolymers and lipids for drug encapsulation.

Soft Matter ◽  
2020 ◽  
Vol 16 (1) ◽  
pp. 142-151 ◽  
Author(s):  
Haiyan Luo ◽  
Kun Jiang ◽  
Xiangfeng Liang ◽  
Huizhou Liu ◽  
Yingbo Li

The influence of hydrogen bonding on the morphological transition of Pluronic P123 micelles is experimentally and theoretically investigated by introducing three small molecules, i.e. propyl benzoate (PB), propyl paraben (PP) and propyl gallate (PG).


2016 ◽  
Vol 4 (44) ◽  
pp. 7119-7129 ◽  
Author(s):  
Deepak Kakde ◽  
Vincenzo Taresco ◽  
Kuldeep K. Bansal ◽  
E. Peter Magennis ◽  
Steven M. Howdle ◽  
...  

Block co-polymers with a block derived from a sustainable monomer source are used to encapsulate and release the drug indomethacin.


2019 ◽  
Vol 223 ◽  
pp. 115118 ◽  
Author(s):  
Magdalena C. Stanciu ◽  
Marieta Nichifor ◽  
Georgeta Mocanu ◽  
Cristina Tuchilus ◽  
Gabriela L. Ailiesei

2013 ◽  
Vol 19 (4) ◽  
pp. 205-213 ◽  
Author(s):  
Susanna Sartori ◽  
Andrea Caporale ◽  
Alfonsina Rechichi ◽  
Domenico Cufari ◽  
Caterina Cristallini ◽  
...  

2005 ◽  
Vol 26 (24) ◽  
pp. 1918-1924 ◽  
Author(s):  
Michael A. R. Meier ◽  
Sebastianus N. H. Aerts ◽  
Bastiaan B. P. Staal ◽  
Mircea Rasa ◽  
Ulrich S. Schubert

2013 ◽  
Vol 14 (5) ◽  
pp. 1555-1563 ◽  
Author(s):  
Zeng-Ying Qiao ◽  
Ran Ji ◽  
Xiao-Nan Huang ◽  
Fu-Sheng Du ◽  
Rui Zhang ◽  
...  

Author(s):  
G.P.A. Vigers ◽  
R.A. Crowther ◽  
B.M.F. Pearse

Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.


2002 ◽  
Vol 724 ◽  
Author(s):  
Elizabeth R. Wright ◽  
R. Andrew McMillan ◽  
Alan Cooper ◽  
Robert P. Apkarian ◽  
Vincent P. Conticello

AbstractTriblock copolymers have traditionally been synthesized with conventional organic components. However, triblock copolymers could be synthesized by the incorporation of two incompatible protein-based polymers. The polypeptides would differ in their hydrophobicity and confer unique physiochemical properties to the resultant materials. One protein-based polymer, based on a sequence of native elastin, that has been utilized in the synthesis of biomaterials is poly (Valine-Proline-Glycine-ValineGlycine) or poly(VPGVG) [1]. This polypeptide has been shown to have an inverse temperature transition that can be adjusted by non-conservative amino acid substitutions in the fourth position [2]. By combining polypeptide blocks with different inverse temperature transition values due to hydrophobicity differences, we expect to produce amphiphilic polypeptides capable of self-assembly into hydrogels. Our research examines the design, synthesis and characterization of elastin-mimetic block copolymers as functional biomaterials. The methods that are used for the characterization include variable temperature 1D and 2D High-Resolution-NMR, cryo-High Resolutions Scanning Electron Microscopy and Differential Scanning Calorimetry.


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