scholarly journals Insight into the binding of a non-toxic, self-assembling aromatic tripeptide with ct-DNA: Spectroscopic and viscositic studies

2017 ◽  
Vol 11 ◽  
pp. 112-118 ◽  
Author(s):  
Soumi Biswas ◽  
Satyabrata Samui ◽  
Arpita Chakraborty ◽  
Sagar Biswas ◽  
Debapriya De ◽  
...  
Keyword(s):  
Self Assembling ◽  
Ct Dna ◽  
Insight Into

scholarly journals Structural analysis of cross α-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Fengbin Wang ◽  
Ordy Gnewou ◽  
Charles Modlin ◽  
Leticia C. Beltran ◽  
Chunfu Xu ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Synthetic Peptide ◽  
Quaternary Structure ◽  
De Novo ◽  
Rational Approach ◽  
Lateral Interactions ◽  
Protein Assemblies ◽  
Self Assembling ◽  
Arginine Residues ◽  
Insight Into

AbstractThe exquisite structure-function correlations observed in filamentous protein assemblies provide a paradigm for the design of synthetic peptide-based nanomaterials. However, the plasticity of quaternary structure in sequence-space and the lability of helical symmetry present significant challenges to the de novo design and structural analysis of such filaments. Here, we describe a rational approach to design self-assembling peptide nanotubes based on controlling lateral interactions between protofilaments having an unusual cross-α supramolecular architecture. Near-atomic resolution cryo-EM structural analysis of seven designed nanotubes provides insight into the designability of interfaces within these synthetic peptide assemblies and identifies a non-native structural interaction based on a pair of arginine residues. This arginine clasp motif can robustly mediate cohesive interactions between protofilaments within the cross-α nanotubes. The structure of the resultant assemblies can be controlled through the sequence and length of the peptide subunits, which generates synthetic peptide filaments of similar dimensions to flagella and pili.

scholarly journals β-Cyclodextrin- and adamantyl-substituted poly(acrylate) self-assembling aqueous networks designed for controlled complexation and release of small molecules

2017 ◽  
Vol 13 ◽  
pp. 1879-1892 ◽  
Author(s):  
Liang Yan ◽  
Duc-Truc Pham ◽  
Philip Clements ◽  
Stephen F Lincoln ◽  
Jie Wang ◽  
...  
Keyword(s):  
Methyl Orange ◽  
Small Molecules ◽  
Controlled Drug Release ◽  
Methyl Red ◽  
Dialysis Membrane ◽  
Factors Affecting ◽  
H Nmr ◽  
Self Assembling ◽  
Vis Spectroscopy ◽  
Insight Into

Three aqueous self-assembling poly(acrylate) networks have been designed to gain insight into the factors controlling the complexation and release of small molecules within them. These networks are formed between 8.8% 6A-(2-aminoethyl)amino-6A-deoxy-6A-β-cyclodextrin, β-CDen, randomly substituted poly(acrylate), PAAβ-CDen, and one of the 3.3% 1-(2-aminoethyl)amidoadamantyl, ADen, 3.0% 1-(6-aminohexyl)amidoadamantyl, ADhn, or 2.9% 1-(12-aminododecyl)amidoadamantyl, ADddn, randomly substituted poly(acrylate)s, PAAADen, PAAADhn and PAAADddn, respectively, such that the ratio of β-CDen to adamantyl substituents is ca. 3:1. The variation of the characteristics of the complexation of the dyes methyl red, methyl orange and ethyl orange in these three networks and by β-cyclodextrin, β-CD, and PAAβ-CDen alone provides insight into the factors affecting dye complexation. The rates of release of the dyes through a dialysis membrane from the three aqueous networks show a high dependence on host–guest complexation between the β-CDen substituents and the dyes as well as the structure and the viscosity of the network as shown by ITC, 1H NMR and UV–vis spectroscopy, and rheological studies. Such networks potentially form a basis for the design of controlled drug release systems.

Tuning the polarity and surface activity of hydroxythiazoles – extending the applicability of highly fluorescent self-assembling chromophores to supra-molecular photonic structures

2016 ◽  
Vol 4 (5) ◽  
pp. 958-971 ◽  
Author(s):  
S. H. Habenicht ◽  
S. Schramm ◽  
S. Fischer ◽  
T. Sachse ◽  
F. Herrmann-Westendorf ◽  
...  
Keyword(s):  
Thin Films ◽  
Optical Properties ◽  
Surface Activity ◽  
Langmuir Blodgett ◽  
Photonic Structures ◽  
Self Assembling ◽  
Insight Into

Processing of 4-alkoxythiazole sulfonamidesviathe Langmuir–Blodgett technique gave an insight into the influence of aggregation on the electro-optical properties of thin films.

scholarly journals Insight into the esterase like activity demonstrated by an imidazole appended self-assembling hydrogelator

2015 ◽  
Vol 51 (67) ◽  
pp. 13213-13216 ◽  
Author(s):  
Nishant Singh ◽  
Maria P. Conte ◽  
R. V. Ulijn ◽  
Juan F. Miravet ◽  
Beatriu Escuder
Keyword(s):  
Methyl Ester ◽  
Self Assembling ◽  
Phenylalanine Methyl Ester ◽  
First Time ◽  
Hydrolysis Of ◽  
Insight Into

Hydrolysis of unactivated phenylalanine methyl ester by a simple imidazole appended hydrogelator is reported for the first time.

scholarly journals Insight into the Self-Assembling Properties of a Peptergent: A Molecular Dynamics Study

2018 ◽  
Author(s):  
Jean-Marc Crowet ◽  
Mehmet Nail Nasir ◽  
Antoine Deschamps ◽  
Vincent Stroobant ◽  
Pierre Morsomme ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Membrane Proteins ◽  
Chemical Properties ◽  
Beta Sheets ◽  
The Self ◽  
Self Assembling ◽  
Beta Barrel ◽  
Physico Chemical ◽  
Ordered Nanostructures ◽  
Insight Into

By manipulating the various physico-chemical properties of amino acids, design of peptides with specific self-assembling properties has been emerging since more than a decade. In this context, short peptides possessing detergent properties (so-called “peptergents”) have been developed to self-assemble into well-ordered nanostructures that can stabilize membrane proteins for crystallization. In this study, the peptide with “peptergency” properties, called ADA8 extensively described by Zhang et al., is studied by molecular dynamics for its self-assembling properties in different conditions. In water, it spontaneously forms beta sheets with a β barrel-like structure. We next simulated the interaction of this peptide with a membrane protein, the bacteriorhodopsin, in the presence or absence of a micelle of dodecylphosphocholine. According to the literature, the peptergent ADA8 is thought to generate a belt of β structures around the hydrophobic helical domain that could help stabilize purified membrane proteins. Molecular dynamics is here used to challenge this view and to provide further molecular details for the replacement of detergent molecules around the protein. To our best knowledge, this is the first molecular mechanism proposed for ''peptergency''. In addition, our calculation approach should serve as a predicting tool for the design of beta peptergent with diverse amphipathic properties.

SYNTHESIS AND BIOLOGICAL ACTIVITY OF THE NEW PINCER TYPE RUTHENIUM(III) COMPLEX

2021 ◽  
Author(s):  
Ana Rilak Simović ◽  
◽  
Dejan Lazić ◽  
Milica Međedović ◽  
Dušan Ćoćić ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
The Other ◽  
Substitution Reactions ◽  
Biological Targets ◽  
Type Complex ◽  
Calf Thymus ◽  
Vis Spectroscopy ◽  
The Spectator ◽  
Ct Dna ◽  
Insight Into

We synthesized and characterized the ruthenium(III) pincer-type complex [RuCl3(H2Lt-Bu] (H2Lt- Bu = 2,6-bis(5-tert-butyl-1H-pyrazol-3-yl)pyridine, 1) by elemental analysis, IR and UV-Vis spectroscopy, and mass spectrometry (MS) method ESI Q-TOF. For comparison reason, we also studied ruthenium(III) terpyridine complexes of the general formula [Ru(N-N-N)Cl3] where N-N-N = 4′-chloro- terpyridine (Cl-tpy; 2) or 4′-chlorophenyl-terpyridine (Cl-Ph-tpy; 3). Kinetic study of the substitution reactions of 1–3 with biomolecules showed that the rate constants depend on the properties of the spectator ligand and the nature of the entering nucleophile. To gain further insight into the reactivity of ruthenium complexes with potential biological targets, we examined the interactions of 1 – 3 with DNA and HSA. The DNA/HSA binding study showed that in comparison to complex 1 (bis– pyrazolylpyridine), the other two (2 and 3) terpyridine complexes had a slightly better binding affinity to calf thymus DNA (CT DNA), while in the case of human serum albumin (HSA), complex 1 exhibited the most strong quenching ability.

α-Hemolysin: A Self-Assembling Protein Pore With Potential Applications In The Synthesis of New Materials

1991 ◽  
Vol 255 ◽  
Author(s):  
Hagan Bayley ◽  
Musti Krishnasastry ◽  
Barbara Walker ◽  
John Kasianowicz
Keyword(s):  
Genetic Manipulation ◽  
Internal Diameter ◽  
New Materials ◽  
Membrane Pores ◽  
Self Assembling ◽  
Assembly Mechanism ◽  
Potential Applications ◽  
Membrane Bound ◽  
Insight Into ◽  
Selection Of

AbstractA selection of nanoscale membrane pores is being constructed by genetic manipulation of α-hemolysin (αHL), a 33.2 kDa polypeptide secreted by the bacterium Staphylococcus aureus, which can self-assemble into hexameric cylindrical channels -1 to 2 nm In Internal diameter. Ultimately, the new pores will be used to confer novel permeability properties upon materials such as thin films utilizing, for example, monolayer sheets of the hexamer. Recombinant αHL (r-αHL) has now been obtained in multimilligram amounts and purified to homogeneity after overexpression of the αHL gene in Escherichia coli. The properties of r-αHL are closely similar to those of αHL purified from S. aureus. Recent deletion mutagenesis experiments have given us new insight into the assembly mechanism of the pore. Three intermediates have been identified: a membrane-bound monomer; an oligomeric pore precursor; and the hexameric pore itself. Currently, point mutogenesis combined with chemical modification is being used to produce new pores of different internal diameter, with selectivity for the passage of molecules and Ions, and with gating properties (the ability to open and close in response to a physical stimulus, e.g. an electric field or light).

scholarly journals Allosteric pathway selection in templated assembly

2019 ◽  
Vol 5 (10) ◽  
pp. eaaw3353 ◽  
Author(s):  
Martijn van Galen ◽  
Ruben Higler ◽  
Joris Sprakel
Keyword(s):  
Building Blocks ◽  
Supramolecular Interactions ◽  
High Fidelity ◽  
Self Assembling ◽  
Molecular Building Blocks ◽  
Large Numbers ◽  
Solution Aggregation ◽  
Allosteric Pathway ◽  
Insight Into ◽  
Selection Of

Assembling large numbers of molecular building blocks into functional nanostructures is no trivial task. It relies on guiding building blocks through complex energy landscapes shaped by synergistic and antagonistic supramolecular interactions. In nature, the use of molecular templates is a potent strategy to navigate the process to the desired structure with high fidelity. Yet, nature’s templating strategy remains to be fully exploited in man-made nanomaterials. Designing effective template-guided self-assembling systems can only be realized through precise insight into how the chemical design of building blocks and the resulting balance of repulsive and attractive forces give rise to pathway selection and suppression of trapped states. We develop a minimal model to unravel the kinetic pathways and pathway selection of the templated assembly of molecular building blocks on a template. We show how allosteric activation of the associative interactions can suppress undesired solution-aggregation pathways and gives rise to a true template-assembly path.

scholarly journals Decoding the absolute stoichiometric composition and structural plasticity of α-carboxysomes

2021 ◽  
Author(s):  
Yaqi Sun ◽  
Victoria M. Harman ◽  
James R. Johnson ◽  
Taiyu Chen ◽  
Gregory F. Dykes ◽  
...  
Keyword(s):  
Rational Design ◽  
Carbon Fixation ◽  
Stoichiometric Composition ◽  
Quantitative Mass Spectrometry ◽  
Shell Protein ◽  
Self Assembling ◽  
The Absolute ◽  
Halothiobacillus Neapolitanus ◽  
Protein Shell ◽  
Insight Into

AbstractCarboxysomes are anabolic bacterial microcompartments that play an essential role in carbon fixation in cyanobacteria and some chemoautotrophs. This self-assembling organelle encapsulates the key CO2-fixing enzymes, Rubisco, and carbonic anhydrase using a polyhedral protein shell that is constructed by hundreds of shell protein paralogs. The α-carboxysome from the chemoautotroph Halothiobacillus neapolitanus serves as a model system in fundamental studies and synthetic engineering of carboxysomes. Here we adopt a QconCAT-based quantitative mass spectrometry to determine the absolute stoichiometric composition of native α-carboxysomes from H. neapolitanus. We further performed an in-depth comparison of the protein stoichiometry of native and recombinant α-carboxysomes heterologously generated in Escherichia coli to evaluate the structural variability and remodeling of α-carboxysomes. Our results provide insight into the molecular principles that mediate carboxysome assembly, which may aid in rational design and reprogramming of carboxysomes in new contexts for biotechnological applications.

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