Impact of Polymer Microstructure on the Self-Assembly of Amphiphilic Polymers in Aqueous Solutions

2007 ◽  
Vol 40 (12) ◽  
pp. 4276-4286 ◽  
Author(s):  
Roger C. W. Liu ◽  
Agnès Pallier ◽  
Marc Brestaz ◽  
Nadège Pantoustier ◽  
Christophe Tribet
Keyword(s):  
Aqueous Solutions ◽  
Self Assembly ◽  
Amphiphilic Polymers ◽  
The Self ◽  
Polymer Microstructure

Chemical controls on uranyl citrate speciation and the self-assembly of nanoscale macrocycles and sandwich complexes in aqueous solutions

2015 ◽  
Vol 51 (25) ◽  
pp. 5306-5309 ◽  
Author(s):  
M. Basile ◽  
D. K. Unruh ◽  
K. Gojdas ◽  
E. Flores ◽  
L. Streicher ◽  
...  
Keyword(s):  
Aqueous Solutions ◽  
Structural Characterization ◽  
Self Assembly ◽  
Spectroscopic Studies ◽  
The Self ◽  
Sandwich Complexes

Speciation and molecular self-assembly of uranyl citrate complexes have been determined based upon structural characterization and spectroscopic studies.

The influence of directed hydrogen bonds on the self-assembly of amphiphilic polymers in water

2019 ◽  
Vol 557 ◽  
pp. 488-497 ◽  
Author(s):  
Tobias Klein ◽  
Franka V. Gruschwitz ◽  
Sarah Rogers ◽  
Stephanie Hoeppener ◽  
Ivo Nischang ◽  
...  
Keyword(s):  
Hydrogen Bonds ◽  
Self Assembly ◽  
Amphiphilic Polymers ◽  
The Self

scholarly journals New Insights on the Self-Assembly of Bio-sourced Block Copolymer MH-b-PS in Aqueous Solutions: Nanocorals, Cubosomes & Nanocubes

2021 ◽  
Author(s):  
Yomen Atassi ◽  
Redouane Borsali
Keyword(s):  
Aqueous Solution ◽  
Block Copolymer ◽  
Aqueous Solutions ◽  
Self Assembly ◽  
Room Temperature ◽  
Linear Structure ◽  
The Self ◽  
Fine Tuning ◽  
Experimental Parameters ◽  
First Time

Polymer self-assembly in solution still constitutes a simple methodology for the preparation of elegant yet sophisticated nanomaterials. This work aims at presenting how the fine tuning of the experimental parameters of the nanoprecipitation process can lead to a variety of novel morphologies ranging from nanocorals through cubosomes to nanocubes. A carbohydrate dibloc copolymer with a simple and linear structure MH1.2k-b-PS2.3 has been used as a model to illustrate the formation of these new self-assemblies. This is the first time that nanocube morphology has been generated using this type of bio-sourced co-polymer in aqueous solution and at room temperature.

Characterization of the Self-Assembly of meso-Tetra(4-sulfonatophenyl)porphyrin (H2TPPS4–) in Aqueous Solutions

2011 ◽  
Vol 13 (1) ◽  
pp. 60-72 ◽  
Author(s):  
Javoris V. Hollingsworth ◽  
Allison J. Richard ◽  
M. Graça H. Vicente ◽  
Paul S. Russo
Keyword(s):  
Aqueous Solutions ◽  
Self Assembly ◽  
The Self

The relationship between molecular structure and supramolecular morphology in the self-assembly of rod–coil molecules with oligoether chains

Soft Matter ◽  
2020 ◽  
Vol 16 (9) ◽  
pp. 2224-2229
Author(s):  
Jie Lu ◽  
Shengsheng Yu ◽  
Zhaohua Li ◽  
Myongsoo Lee ◽  
Yuntian Yang ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Aqueous Solutions ◽  
Self Assembly ◽  
The Self ◽  
Methyl Groups ◽  
The Relationship

Supramolecular nanoassemblies such as scrolled/helical nanofibers and nanorings were constructed by controlling the length of the oligoether chains and inserting lateral methyl groups at the surface of the rod and coil domains in aqueous solutions.

The Nature of Rapidly Extracted Phycocyanin from the Blue-Green Alga Plectonema Boryanum

1971 ◽  
Vol 29 ◽  
pp. 366-367
Author(s):  
M. Kessel ◽  
R. MacColl
Keyword(s):  
Self Assembly ◽  
Analytical Ultracentrifugation ◽  
Uranyl Acetate ◽  
The Self ◽  
Major Protein ◽  
Subunit Structure ◽  
Blue Green Alga ◽  
Thin Sections ◽  
Blue Green Algae ◽  
Cacodylate Buffer

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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