Synthetic approaches to construct viral capsid-like spherical nanomaterials

2018 ◽  
Vol 54 (65) ◽  
pp. 8944-8959 ◽  
Author(s):  
Kazunori Matsuura
Keyword(s):  
Self Assembly ◽  
Recent Progress ◽  
The Self ◽  
Viral Capsid ◽  
Feature Article ◽  
Synthetic Approaches

This feature article describes recent progress in synthetic strategies to construct viral capsid-like spherical nanomaterials using the self-assembly of peptides and/or proteins.

Identification of a major intermediate along the self-assembly pathway of an icosahedral viral capsid by using an analytical model of a spherical patch

Soft Matter ◽  
2016 ◽  
Vol 12 (32) ◽  
pp. 6728-6736 ◽  
Author(s):  
Didier Law-Hine ◽  
Mehdi Zeghal ◽  
Stéphane Bressanelli ◽  
Doru Constantin ◽  
Guillaume Tresset
Keyword(s):  
Analytical Model ◽  
Self Assembly ◽  
The Self ◽  
Viral Capsid ◽  
Assembly Pathway

Designing soft nanomaterials via the self assembly of functionalized icosahedral viral capsid nanoparticles

2014 ◽  
Vol 30 (1) ◽  
pp. 141-150 ◽  
Author(s):  
Vidyalakshmi Chockalingam Muthukumar ◽  
Leebyn Chong ◽  
Meenakshi Dutt
Keyword(s):  
Self Assembly ◽  
The Self ◽  
Viral Capsid ◽  
Image Position

Abstract

scholarly journals Hot Spots and Their Contribution to the Self-Assembly of the Viral Capsid: In Silico Prediction and Analysis

2019 ◽  
Vol 20 (23) ◽  
pp. 5966 ◽  
Author(s):  
Armando Díaz-Valle ◽  
José Marcos Falcón-González ◽  
Mauricio Carrillo-Tripp
Keyword(s):  
Free Energy ◽  
Self Assembly ◽  
Hot Spots ◽  
Binding Free Energy ◽  
Hot Spot ◽  
Free Energy Calculations ◽  
The Self ◽  
Viral Capsid ◽  
Macromolecular Complex ◽  
Single Mutation

The viral capsid is a macromolecular complex formed by a defined number of self-assembled proteins, which, in many cases, are biopolymers with an identical amino acid sequence. Specific protein–protein interactions (PPI) drive the capsid self-assembly process, leading to several distinct protein interfaces. Following the PPI hot spot hypothesis, we present a conservation-based methodology to identify those interface residues hypothesized to be crucial elements on the self-assembly and thermodynamic stability of the capsid. We validate the predictions through a rigorous physical framework which integrates molecular dynamics simulations and free energy calculations by Umbrella sampling and the potential of mean force using an all-atom molecular representation of the capsid proteins of an icosahedral virus in an explicit solvent. Our results show that a single mutation in any of the structure-conserved hot spots significantly perturbs the quaternary protein–protein interaction, decreasing the absolute value of the binding free energy, without altering the protein’s secondary nor tertiary structure. Our conservation-based hot spot prediction methodology can lead to strategies to rationally modulate the capsid’s thermodynamic properties.

Recent developments in the construction of metallacycle/metallacage-cored supramolecular polymers via hierarchical self-assembly

2019 ◽  
Vol 55 (56) ◽  
pp. 8036-8059 ◽  
Author(s):  
Bo Li ◽  
Tian He ◽  
Yiqi Fan ◽  
Xinchao Yuan ◽  
Huayu Qiu ◽  
...  
Keyword(s):  
Self Assembly ◽  
Recent Progress ◽  
Supramolecular Polymers ◽  
Feature Article ◽  
Light Emitting ◽  
Recent Developments ◽  
Potential Applications ◽  
Bio Imaging

This feature article summarized the recent progress on the construction of metallacycle/metallacage-cored supramolecular polymers by the hierarchical self-assembly, and the potential applications in the areas of light emitting, sensing, bio-imaging, delivery and release, etc., are also presented.

scholarly journals Hot-spots and their contribution to the self-assembly of the viral capsid: in-vitro validation

2019 ◽  
Author(s):  
Alejandra Gabriela Valdez-Lara ◽  
Mariana Andrade-Medina ◽  
Josué Alejandro Alemán-Vilis ◽  
Aldo Adrián Pérez-Montoya ◽  
Nayely Pineda-Aguilar ◽  
...  
Keyword(s):  
Self Assembly ◽  
Hot Spots ◽  
Point Mutations ◽  
The Self ◽  
Viral Capsid ◽  
Single Mutation ◽  
Chlorotic Mottle Virus ◽  
Chlorotic Mottle ◽  
Interface Residues

AbstractThe viral capsid is a macromolecular complex formed by self-assembled proteins (CPs) which, in many cases, are biopolymers with an identical amino acid sequence. Specific CP-CP interactions drive the capsid self-assembly process. However, it is believed that only a small set of protein-protein interface residues significantly contribute to the formation of the capsid; the so-called “hot-spots”. Here, we investigate the effect of in-vitro point-mutations on the Bromoviridae family structure-conserved interface residues of the icosahedral Cowpea Chlorotic Mottle Virus, previously hypothesized as hot-spots. We study the self-assembly of those mutated recombinant CPs for the formation of capsids by Thermal Shift Assay (TSA). We show that the TSA biophysical technique is a reliable way to characterize capsid assembly. Our results show that point-mutations on non-conserved interface residues produce capsids indistinguishable from the wild-type. In contrast, a single mutation on structure-conserved residues E176 or V189 prevents the formation of the capsid while maintaining the tertiary fold of the CP. Our findings provide experimental evidence of the in-silico conservation-based hot-spot prediction accuracy. As a whole, our methodology provides a framework that could aid in the rational development of molecules to inhibit virus formation, or advance capsid bioengineering to design for their stability, function and applications.

scholarly journals Recent Progress in the Fabrication of Low Dimensional Nanostructures via Surface-Assisted Transforming and Coupling

2017 ◽  
Vol 2017 ◽  
pp. 1-17 ◽  
Author(s):  
Jinbang Hu ◽  
Zhaofeng Liang ◽  
Kongchao Shen ◽  
Haoliang Sun ◽  
Zheng Jiang ◽  
...  
Keyword(s):  
Phase Transformations ◽  
Self Assembly ◽  
Recent Progress ◽  
Solid Surfaces ◽  
Ullmann Reaction ◽  
Surface Polymerization ◽  
Low Dimensional ◽  
Synthetic Approaches ◽  
2D Network ◽  
Selection Of

Polymerization of functional organics into covalently cross-linked nanostructures via bottom-up approach on solid surfaces has attracted tremendous interest recently, due to its appealing potentials in fabricating novel and artificial low dimensional nanomaterials. While there are various synthetic approaches being proposed and explored, this paper reviews the recent progress of on-surface coupling strategies towards the synthesis of low dimensional nanostructures ranging from 1D nanowire to 2D network and describes their advantages and drawbacks during on-surface process and phase transformations, for example, from molecular self-assembly to on-surface polymerization. Specifically, Ullmann reaction is discussed in detail and the mechanism governing nanostructures’ transforming effect by surface treatment is exploited. In the end, it is summarized that the hierarchical polymerization combined with Ullmann coupling makes it possible to realize the selection of different synthetic pathways and phase transformations and obtain novel organometallic nanowire with metalorganic bonding.

Recent progress in the self-assembly of block copolymers confined in emulsion droplets

2018 ◽  
Vol 54 (94) ◽  
pp. 13183-13195 ◽  
Author(s):  
Nan Yan ◽  
Yutian Zhu ◽  
Wei Jiang
Keyword(s):  
Block Copolymers ◽  
Self Assembly ◽  
Recent Progress ◽  
The Self ◽  
Confinement Effect ◽  
Emulsion Droplet ◽  
Emulsion Droplets

When the self-assembly of block copolymers (BCPs) occurs within a deformable emulsion droplet, BCPs can aggregate into a variety of nanoscaled particles with unique nanostructures and properties since the confinement effect can effectively break the symmetry of a structure.

scholarly journals Hot-spots and their contribution to the self-assembly of the viral capsid: in-silico prediction and analysis

2019 ◽  
Author(s):  
Armando Díaz-Valle ◽  
José Marcos Falcón-González ◽  
Mauricio Carrillo-Tripp
Keyword(s):  
Free Energy ◽  
Self Assembly ◽  
Hot Spots ◽  
Binding Free Energy ◽  
Free Energy Calculations ◽  
The Self ◽  
Atomic Scale ◽  
Viral Capsid ◽  
Macromolecular Complex ◽  
Single Mutation

AbstractIn order to rationally design biopolymers that mimic biological functions, first, we need to elucidate the molecular mechanisms followed by nature. For example, the viral capsid is a macromolecular complex formed by self-assembled proteins which, in many cases, are biopolymers with an identical amino acid sequence. Specific protein-protein interactions drive the capsid self-assembly process, leading to several distinct protein interfaces. Following the hot-spot hypothesis, we propose a conservation-based methodology to identify those interface residues that are crucial elements on the self-assembly and thermodynamic stability of the capsid. We validate our predictions by computational free energy calculations using an atomic-scale molecular model of an icosahedral virus. Our results show that a single mutation in any of the hot-spots significantly perturbs the quaternary interaction, decreasing the absolute value of the binding free energy, without altering the tertiary structure. Our methodology can lead to a strategy to rationally modulate the capsid’s thermodynamic properties.

scholarly journals Recent Progress and Future Challenges in the Supramolecular Polymerization of Metal-containing Monomers

2021 ◽  
Author(s):  
Nils Bäumer ◽  
Jonas Matern ◽  
Gustavo Fernandez
Keyword(s):  
Self Assembly ◽  
Recent Progress ◽  
Research Area ◽  
The Self ◽  
Functional Nanomaterials ◽  
Major Research ◽  
The Past ◽  
Future Challenges ◽  
Supramolecular Polymerization

The self-assembly of discrete molecular entities into functional nanomaterials has become a major research area in the past decades. The library of investigated compounds has diversified significantly, while the field...

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