Self-assembly of ionic and non-ionic surfactants in type IV cerium nitrate and urea based deep eutectic solvent

2021 ◽  
Vol 155 (8) ◽  
pp. 084902
Author(s):  
Iva Manasi ◽  
Mohammad R. Andalibi ◽  
Ria S. Atri ◽  
Jake Hooton ◽  
Stephen M. King ◽  
...  
Keyword(s):  
Self Assembly ◽  
Deep Eutectic Solvent ◽  
Cerium Nitrate ◽  
Ionic Surfactants ◽  
Type Iv

scholarly journals Heparin type IV collagen interactions: equilibrium binding and inhibition of type IV collagen self-assembly.

1988 ◽  
Vol 263 (35) ◽  
pp. 19112-19118 ◽  
Author(s):  
E C Tsilibary ◽  
G G Koliakos ◽  
A S Charonis ◽  
A M Vogel ◽  
L A Reger ◽  
...  
Keyword(s):  
Self Assembly ◽  
Type Iv Collagen ◽  
Type Iv ◽  
Equilibrium Binding

scholarly journals Inhibition of laminin self-assembly and interaction with type IV collagen by antibodies to the terminal domain of the long arm.

1986 ◽  
Vol 103 (5) ◽  
pp. 1689-1697 ◽  
Author(s):  
A S Charonis ◽  
E C Tsilibary ◽  
T Saku ◽  
H Furthmayr
Keyword(s):  
Self Assembly ◽  
Binding Sites ◽  
Type Iv Collagen ◽  
Specific Interaction ◽  
Basement Membranes ◽  
Complex Domain ◽  
Peptide Fragment ◽  
Type Iv ◽  
Collagen Molecules

Laminin is a major glycoprotein of the basement membrane. Although its precise localization and orientation within this structure is unknown, it is presumably anchored to other macromolecules such as type IV collagen or proteoheparan sulfate. In vitro, laminin has the ability to self-assemble and to bind to type IV collagen molecules at distinct sites. To identify more precisely the domains of the complex, cross-shaped laminin molecule that are involved in these interactions, images of laminin-laminin dimers and laminin-type IV collagen complexes obtained by the rotary shadowing method were analyzed. We observed that the complex domain at the end of the long arm of laminin is predominantly involved in these interactions. By using Fab fragments of antibodies specific for a peptide fragment derived from this complex domain, it is shown that laminin self-assembly is inhibited in their presence, as measured by turbidity and by electron microscopy. In addition, these antibodies inhibit the specific interaction of laminin with type IV collagen. These data suggest that the complex domain at the end of the long arm of laminin contains binding sites of potential importance for the assembly of basement membranes.

Biomorphic Mesoporous Ce1−xZrxO2 Nanostructures Fabricated from Paper Templates

2008 ◽  
Vol 1094 ◽  
Author(s):  
Dickon H. L. Ng ◽  
Jia Li
Keyword(s):  
Grain Size ◽  
Hydroxyl Radicals ◽  
Self Assembly ◽  
The Self ◽  
Cerium Nitrate ◽  
Zirconium Nitrate ◽  
Paper Structure ◽  
Nitrate Solutions

AbstractA simple and versatile procedure was developed for synthesizing biomorphic mesoporous Ce1-xZrxO2. Aqueous cerium nitrate and zirconium nitrate solutions, and paper were used as the starting materials. Under the structure-directed effect offered by the active hydroxyl radicals of the cellulose in the paper templates, porous and fibrous structures of paper were replicated by the self-assembly of Ce1-xZrxO2 nanocrystallites after the paper underwent chemical infiltration and calcinations. The product, composing of interwoven network of fibers with diameter ranging from 10 to 20 <mu>m, was a replica of the original paper structure only that each fiber was assembled by Ce1-xZrxO2 nanocrystallites with grain size of 3-10 nm. The templating function of cellulose and the mechanism in the formation of nanocrystallites were proposed.

Self-assembly of coarse-grained ionic surfactants accelerated by graphics processing units

Soft Matter ◽  
2012 ◽  
Vol 8 (8) ◽  
pp. 2385-2397 ◽  
Author(s):  
David N. LeBard ◽  
Benjamin G. Levine ◽  
Philipp Mertmann ◽  
Stephen A. Barr ◽  
Arben Jusufi ◽  
...  
Keyword(s):  
Self Assembly ◽  
Graphics Processing Units ◽  
Coarse Grained ◽  
Ionic Surfactants ◽  
Graphics Processing

Quaternary Type IV Deep Eutectic Solvent-Based Tungsten Oxide/Niobium Oxide Photochromic and Reverse Fading Composite Complex

2021 ◽  
Author(s):  
Onome Ejeromedoghene ◽  
Xiangyu Ma ◽  
Olayinka Oderinde ◽  
Fang Yao ◽  
Adewuyi Sheriff ◽  
...  
Keyword(s):  
Tungsten Oxide ◽  
Niobium Oxide ◽  
Deep Eutectic Solvent ◽  
Ambient Conditions ◽  
Solvothermal Route ◽  
Type Iv

A new quaternary type IV deep eutectic solvent (DES) was prepared for the synthesis of WO3/Nb2O5 complexes via a facile solvothermal route under ambient conditions. The PXRD confirms the formation...

scholarly journals Self-assembly and adsorption of cetyltrimethylammonium bromide and didodecyldimethylammonium bromide surfactants at the mica–water interface

Soft Matter ◽  
2019 ◽  
Vol 15 (41) ◽  
pp. 8402-8411 ◽  
Author(s):  
Georgia Tsagkaropoulou ◽  
Finian J. Allen ◽  
Stuart M. Clarke ◽  
Philip J. Camp
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Self Assembly ◽  
Cetyltrimethylammonium Bromide ◽  
Ionic Surfactants ◽  
Water Interface ◽  
Didodecyldimethylammonium Bromide ◽  
Dynamics Simulations ◽  
Shed Light

Molecular-dynamics simulations are used to explore bilayers formed by simple ionic surfactants at the mica–water interface, and to shed light on experimental observations.

Self-assembly phenomena in multicomponent systems composed of polyelectrolytes and ionic surfactants

1996 ◽  
Vol 106 (1) ◽  
pp. 397-409 ◽  
Author(s):  
Alexander B. Zezin ◽  
Vladimir A. Izumrudov ◽  
Victor A. Kabanov
Keyword(s):  
Self Assembly ◽  
Ionic Surfactants ◽  
Multicomponent Systems

Analysis of the roles of the head domains of type IV rat neuronal intermediate filament proteins in filament assembly using domain-swapped chimeric proteins

1999 ◽  
Vol 112 (13) ◽  
pp. 2233-2240
Author(s):  
G.Y. Ching ◽  
R.K. Liem
Keyword(s):  
Intermediate Filament ◽  
Self Assembly ◽  
Chimeric Proteins ◽  
Filament Formation ◽  
Intermediate Filament Proteins ◽  
L Protein ◽  
Type Iv ◽  
Filament Assembly ◽  
Head Domain ◽  
Neuronal Intermediate Filament Proteins

Type IV neuronal intermediate filament proteins consist of alpha-internexin, which can self-assemble into filaments and the neurofilament triplet proteins, which are obligate heteropolymers, at least in rodents. These IF proteins therefore provide good systems for elucidating the mechanism of intermediate filament assembly. To analyze the roles of the head domains of these proteins in contributing to their differential assembly properties, we generated chimeric proteins by swapping the head domains between rat alpha-internexin and either rat NF-L or NF-M and examined their assembly properties in transfected cells that lack their own cytoplasmic intermediate filament network. Lalphaalpha and Malphaalpha, the chimeric proteins generated by replacing the head domain of alpha-internexin with those of NF-L and NF-M, respectively, were unable to self-assemble into filaments. In contrast, alphaLL, a chimeric NF-L protein generated by replacing the head domain of NF-L with that of alpha-internexin, was able to self-assemble into filaments, whereas MLL, a chimeric NF-L protein containing the NF-M head domain, was unable to do so. These results demonstrate that the alpha-internexin head domain is essential for alpha-internexin's ability to self-assemble. While coassembly of Lalphaalpha with NF-M and coassembly of Malphaalpha with NF-L resulted in formation of filaments, coassembly of Lalphaalpha with NF-L and coassembly of Malphaalpha with NF-M yielded punctate patterns. These coassembly results show that heteropolymeric filament formation requires that one partner has the NF-L head domain and the other partner has the NF-M head domain. Thus, the head domains of rat NF-L and NF-M play important roles in determining the obligate heteropolymeric nature of filament formation. The data obtained from these self-assembly and coassembly studies provide some new insights into the mechanism of intermediate filament assembly.

Unconventional collagens

2000 ◽  
Vol 113 (23) ◽  
pp. 4141-4142
Author(s):  
D.P. Knight
Keyword(s):  
Connective Tissue ◽  
Self Assembly ◽  
Protein Profile ◽  
Vital Role ◽  
Post Translational Modification ◽  
Connective Tissues ◽  
Sequence Structure ◽  
Oxford University ◽  
Type Iv ◽  
Modular Domain

Unconventional Collagens Types VI, VII, VIII, IX, X, XIV, XVI and XIX by S. Ricard-Blum, B. Dublet and M. van der Rest Oxford University Press (2000) pp.155. ISBN 0–19-850545-0 35.00 This thoroughly researched monograph in Oxford University Press's ‘Protein Profile Series’ reviews substantially all the significant literature on this interesting and highly important group of proteins. The authors use the term ‘Unconventional Collagens’ for the collagens of higher vertebrate connective tissues which do not, of themselves, form classical fibrils with a 68 nm banding pattern. The authors chose to omit type IV collagen as this, they claim, would have almost doubled the size of the volume. The monograph represents a very considerable achievement in three respects. Firstly it comprehensively reviews the literature on the sequence, structure, expression, post-translational modification, genetics, physiological function and pathology of each separate unconventional collagen. The thoroughness of this review is indicated by the fact that the bibliography contains no fewer than 1196 references. Secondly, the monograph identifies the modular domain structure for each collagen, clearly demonstrating that these proteins are block co-polymers mainly derived in evolution from a small number of ancestral genes. Thirdly, it starts to identify the way in which the different modules of these sticky molecules interact with each other and with other connective tissue components. This is an important start if we are to understand their vital role in the self-assembly processes which occur in embryology, tissue repair and the major degenerative and collagen gene diseases The clearly written and well set out text is supported by excellent micrographs of rotary shadowed molecules and molecular aggregates and a wealth of diagrams and tables. The book has, in my view, three minor shortcomings: a short summary chapter on type IV would enable the non-specialist reader to relate this collagen to the other non-conventional collagens. Concise summaries at the ends of each chapter would orient newcomers to the field. More significantly, apart from the brief introduction, the book lacks an overall synthesis which pulls together the findings of the separate chapters. These slight limitations aside, this book is essential reading for those engaged in connective tissue research and will do much to stimulate further activity in this area. It will also be of considerable interest to tissue engineers, pathologists and embryologists.

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