Self-Assembly in Complex Mixed Surfactant Solutions: The Impact of Dodecyl Triethylene Glycol on Dihexadecyl Dimethyl Ammonium Bromide

Langmuir ◽  
2008 ◽  
Vol 24 (18) ◽  
pp. 10089-10098 ◽  
Author(s):  
I. Tucker ◽  
J. Penfold ◽  
R. K. Thomas ◽  
I. Grillo ◽  
D. F. R. Mildner ◽  
...  
Keyword(s):  
Self Assembly ◽  
Triethylene Glycol ◽  
Ammonium Bromide ◽  
Mixed Surfactant ◽  
Surfactant Solutions ◽  
Dimethyl Ammonium ◽  
The Impact

Photodegradation of Chlorobenzenes in Micellar Aqueous Solutions of Gemini Surfactants

2013 ◽  
Vol 409-410 ◽  
pp. 125-128
Author(s):  
Zheng Hua Wang ◽  
Xu Ming Yang ◽  
Bo Zhi Ren
Keyword(s):  
Gemini Surfactant ◽  
Gemini Surfactants ◽  
Sodium Dodecyl ◽  
Surfactant Solution ◽  
Photochemical Reactions ◽  
Ammonium Bromide ◽  
Surfactant Solutions ◽  
Photodegradation Rate ◽  
Conventional Surfactant ◽  
Dimethyl Ammonium

Photodegradation of 1,2,4-trichlorobenzene (1,2,4-TCB) was examined in one kind of Gemini surfactant solution (ethylene dioctadecyl dimethyl ammonium bromide) and two kinds of conventional surfactant solutions (sodium dodecyl sulfate and polyoxyethylene polyoxypropylene ether). Compared with conventional surfactants, Gemini surfactants make up of two identical or different amphiphilic moieties connected by a spacer group. Under UV irradiation at 254 nm, 1,2,4-trichlorobenzene was decomposed in the three micellar solutions, but the photodegradation rate of 1,2,4-trichlorobenzene in the Gemini surfactant solution was 3.54% and 11.81% higher than those in other two conventional surfactant solutions respectively. Thus, the photochemical reactions of chlorobenzenes can be enhanced in Gemini surfactant solutions.

scholarly journals Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System

2021 ◽  
Vol 22 (6) ◽  
pp. 3098
Author(s):  
Aleksander Strugała ◽  
Jakub Jagielski ◽  
Karol Kamel ◽  
Grzegorz Nowaczyk ◽  
Marcin Radom ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Mosaic Virus ◽  
Capsid Protein ◽  
Self Assembly ◽  
Environmental Changes ◽  
Expression System ◽  
Brome Mosaic Virus ◽  
Virus Like Particles ◽  
Assembly Principles ◽  
The Impact

Virus-like particles (VLPs), due to their nanoscale dimensions, presence of interior cavities, self-organization abilities and responsiveness to environmental changes, are of interest in the field of nanotechnology. Nevertheless, comprehensive knowledge of VLP self-assembly principles is incomplete. VLP formation is governed by two types of interactions: protein–cargo and protein–protein. These interactions can be modulated by the physicochemical properties of the surroundings. Here, we used brome mosaic virus (BMV) capsid protein produced in an E. coli expression system to study the impact of ionic strength, pH and encapsulated cargo on the assembly of VLPs and their features. We showed that empty VLP assembly strongly depends on pH whereas ionic strength of the buffer plays secondary but significant role. Comparison of VLPs containing tRNA and polystyrene sulfonic acid (PSS) revealed that the structured tRNA profoundly increases VLPs stability. We also designed and produced mutated BMV capsid proteins that formed VLPs showing altered diameters and stability compared to VLPs composed of unmodified proteins. We also observed that VLPs containing unstructured polyelectrolyte (PSS) adopt compact but not necessarily more stable structures. Thus, our methodology of VLP production allows for obtaining different VLP variants and their adjustment to the incorporated cargo.

Simulations of Micelle Self-Assembly in Surfactant Solutions

Langmuir ◽  
1996 ◽  
Vol 12 (3) ◽  
pp. 746-753 ◽  
Author(s):  
Bruce J. Palmer ◽  
Jun Liu
Keyword(s):  
Self Assembly ◽  
Surfactant Solutions

scholarly journals Cationic and Biocompatible Polymer/Lipid Nanoparticles as Immunoadjuvants

Pharmaceutics ◽  
2021 ◽  
Vol 13 (11) ◽  
pp. 1859
Author(s):  
Yunys Pérez-Betancourt ◽  
Péricles Marques Araujo ◽  
Bianca de Carvalho Lins Fernandes Távora ◽  
Daniele Rodrigues Pereira ◽  
Eliana Lima Faquim-Mauro ◽  
...  
Keyword(s):  
Immune Responses ◽  
Methyl Methacrylate ◽  
Cationic Lipid ◽  
Lipid Nanoparticles ◽  
Hybrid Nanoparticles ◽  
Ammonium Bromide ◽  
The Novel ◽  
Biocompatible Polymer ◽  
Dimethyl Ammonium ◽  
Oppositely Charged

Nanostructures have been of paramount importance for developing immunoadjuvants. They must be cationic and non-cytotoxic, easily assembling with usually oppositely charged antigens such as proteins, haptens or nucleic acids for use in vaccines. We obtained optimal hybrid nanoparticles (NPs) from the biocompatible polymer poly(methyl methacrylate) (PMMA) and the cationic lipid dioctadecyl dimethyl ammonium bromide (DODAB) by emulsion polymerization of methyl methacrylate (MMA) in the presence of DODAB. NPs adsorbed ovalbumin (OVA) as a model antigen and we determined their adjuvant properties. Interestingly, they elicited high double immune responses of the cellular and humoral types overcoming the poor biocompatibility of DODAB-based adjuvants of the bilayer type. The results suggested that the novel adjuvant would be possibly of use in a variety of vaccines.

scholarly journals Effects of Pathological Mutations on the Prion-Like Polymerisation of MyD88

2018 ◽  
Author(s):  
Ailís O’Carroll ◽  
Brieuc Chauvin ◽  
James Brown ◽  
Ava Meagher ◽  
Joanne Coyle ◽  
...  
Keyword(s):  
Single Molecule ◽  
Self Assembly ◽  
Point Mutations ◽  
Adaptor Protein ◽  
Full Length ◽  
Binary Response ◽  
Death Domain ◽  
Tir Domain ◽  
The Impact

AbstractA novel concept has emerged whereby the higher-order self-assembly of proteins provides a simple and robust mechanism for signal amplification. This appears to be a universal signalling mechanism within the innate immune system, where the recognition of pathogens or danger-associated molecular patterns need to trigger a strong, binary response within cells. Previously, multiple structural studies have been limited to single domains, expressed and assembled at high protein concentrations. We therefore set out to develop new in vitro strategies to characterise the behaviour of full-length proteins at physiological levels. In this study we focus on the adaptor protein MyD88, which contains two domains with different self-assembly properties: a TIR domain that can polymerise similarly to the TIR domain of Mal, and a Death Domain that has been shown to oligomerise with helical symmetry in the Myddosome complex. To visualize the behaviour of full-length MyD88 without purification steps, we use single-molecule fluorescence coupled to eukaryotic cell-free protein expression. These experiments demonstrate that at low protein concentration, only full-length MyD88 forms prion-like polymers. We also demonstrate that the metastability of MyD88 polymerisation creates the perfect binary response required in innate signalling: the system is silenced at normal concentrations but upstream signalling creates a “seed” that triggers polymerisation and amplification of the response. These findings pushed us to re-interpret the role of polymerisation in MyD88-related diseases and we studied the impact of disease-associated point mutations L93P, R196C and L252P/L265P at the molecular level. We discovered that all mutations completely block the ability of MyD88 to polymerise. We also confirm that L252P, a gain-of-function mutation, allows the MyD88 mutant to form extremely stable oligomers, even when expressed at low nanomolar concentrations. Thus, our results are consistent with and greatly add to the findings on the Myddosomes digital ‘all-or-none’ responses and the behaviour of the oncogenic mutation of MyD88.

Thermodynamics of Mixed Surfactant Solutions of N,N′-Bis(dimethyldodecyl)-1,2-ethanediammoniumdibromide with 1-Dodecyl-3-methylimidazolium Bromide

2014 ◽  
Vol 118 (4) ◽  
pp. 1168-1179 ◽  
Author(s):  
Changfei Du ◽  
Dongxing Cai ◽  
Miao Qin ◽  
Peizhu Zheng ◽  
Zhiguo Hao ◽  
...  
Keyword(s):  
Mixed Surfactant ◽  
Surfactant Solutions
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