scholarly journals Protein-, (Poly)peptide-, and Amino Acid-Based Nanostructures Prepared via Polymerization-Induced Self-Assembly

Polymers ◽  
2021 ◽  
Vol 13 (16) ◽  
pp. 2603
Author(s):  
Spyridon Varlas ◽  
Georgia L. Maitland ◽  
Matthew J. Derry
Keyword(s):  
Amino Acid ◽  
Block Copolymer ◽  
Self Assembly ◽  
Vital Role ◽  
Amino Acid Sequences ◽  
Direct Construction ◽  
High Concentrations ◽  
Proteins And Peptides ◽  
Novel Protein

Proteins and peptides, built from precisely defined amino acid sequences, are an important class of biomolecules that play a vital role in most biological functions. Preparation of nanostructures through functionalization of natural, hydrophilic proteins/peptides with synthetic polymers or upon self-assembly of all-synthetic amphiphilic copolypept(o)ides and amino acid-containing polymers enables access to novel protein-mimicking biomaterials with superior physicochemical properties and immense biorelevant scope. In recent years, polymerization-induced self-assembly (PISA) has been established as an efficient and versatile alternative method to existing self-assembly procedures for the reproducible development of block copolymer nano-objects in situ at high concentrations and, thus, provides an ideal platform for engineering protein-inspired nanomaterials. In this review article, the different strategies employed for direct construction of protein-, (poly)peptide-, and amino acid-based nanostructures via PISA are described with particular focus on the characteristics of the developed block copolymer assemblies, as well as their utilization in various pharmaceutical and biomedical applications.

Aqueous Dispersion Polymerization: A New Paradigm for in Situ Block Copolymer Self-Assembly in Concentrated Solution

2011 ◽  
Vol 133 (39) ◽  
pp. 15707-15713 ◽  
Author(s):  
Shinji Sugihara ◽  
Adam Blanazs ◽  
Steven P. Armes ◽  
Anthony J. Ryan ◽  
Andrew L. Lewis
Keyword(s):  
Block Copolymer ◽  
Self Assembly ◽  
Dispersion Polymerization ◽  
Aqueous Dispersion ◽  
New Paradigm ◽  
Concentrated Solution

scholarly journals Charge influences substrate recognition and self-assembly of hydrophobic FG sequences

2016 ◽  
Author(s):  
Wesley G. Chen ◽  
Jacob Witten ◽  
Scott C. Grindy ◽  
Niels Holten-Andersen ◽  
Katharina Ribbeck
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Amino Acid Sequences ◽  
Nuclear Pore ◽  
Selective Binding ◽  
Charged Amino Acids ◽  
Essential Components ◽  
Transport Receptors

AbstractThe nuclear pore complex controls the passage of molecules via hydrophobic phenylalanine-glycine (FG) domains on nucleoporins. Such FG-domains consist of repeating units of FxFG, FG, or GLFG sequences, which can be interspersed with highly charged amino acid sequences. Despite the high density of charge exhibited in certain FG-domains, if and how charge influences FG-domain self-assembly and selective binding of nuclear transport receptors is largely unexplored. Studying how individual charged amino acids contribute to nuclear pore selectivity is challenging with modern in vivo and in vitro techniques due to the complexity of nucleoporin sequences. Here, we present a rationally designed approach to deconstruct essential components of nucleoporins down to 14 amino acid sequences. With these nucleoporin-based peptides, we systematically dissect how charge type and placement of charge influences self-assembly and selective binding of FG-containing gels. Specifically, we find that charge type determines which hydrophobic substrates FG sequences recognize while spatial localization of charge tunes hydrophobic self-assembly and receptor selectivity of FG sequences.

In situ fabrication of multifunctional gold–amino acid superstructures based on self-assembly

2019 ◽  
Vol 55 (27) ◽  
pp. 3967-3970 ◽  
Author(s):  
Xuejiao Yang ◽  
Bohao Yang ◽  
Yuefei Wang ◽  
Wei Qi ◽  
Qiguo Xing ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Amino Acid ◽  
Self Assembly ◽  
Au Nps ◽  
In Situ Fabrication ◽  
Photothermal Effects

Based on self-assembly and biomineralization, Au NPs@ferrocene–tryptophan (Fc-W) superstructures were fabricated, exhibiting efficient photothermal effects and catalytic activity.

Probing Self-Assembly of Cylindrical Morphology Block Copolymer Using in Situ and ex Situ Grazing Incidence Small-Angle X-ray Scattering: The Attractive Case of Graphoepitaxy

2014 ◽  
Vol 47 (20) ◽  
pp. 7221-7229 ◽  
Author(s):  
Mireille Maret ◽  
Raluca Tiron ◽  
Xavier Chevalier ◽  
Patrice Gergaud ◽  
Ahmed Gharbi ◽  
...  
Keyword(s):  
Block Copolymer ◽  
Small Angle ◽  
Self Assembly ◽  
Grazing Incidence ◽  
Ex Situ ◽  
X Ray ◽  
X Ray Scattering ◽  
Attractive Case ◽  
Ray Scattering

scholarly journals In Situ Visualization of Block Copolymer Self-Assembly in Organic Media by Super-Resolution Fluorescence Microscopy

2015 ◽  
Vol 21 (51) ◽  
pp. 18539-18542 ◽  
Author(s):  
Charlotte E. Boott ◽  
Romain F. Laine ◽  
Pierre Mahou ◽  
John R. Finnegan ◽  
Erin M. Leitao ◽  
...  
Keyword(s):  
Block Copolymer ◽  
Fluorescence Microscopy ◽  
Self Assembly ◽  
Super Resolution ◽  
Organic Media ◽  
In Situ Visualization

Evaporation-Induced Block Copolymer Self-Assembly into Membranes Studied by in Situ Synchrotron SAXS

2015 ◽  
Vol 48 (5) ◽  
pp. 1524-1530 ◽  
Author(s):  
Corinna Stegelmeier ◽  
Alexander Exner ◽  
Stephan Hauschild ◽  
Volkan Filiz ◽  
Jan Perlich ◽  
...  
Keyword(s):  
Block Copolymer ◽  
Self Assembly ◽  
Synchrotron Saxs

scholarly journals Pathway Complexity in Supramolecular Porphyrin Self-Assembly at an Immiscible Liquid|Liquid Interface

2021 ◽  
Author(s):  
Iván Robayo-Molina ◽  
Andrés F. Molina-Osorio ◽  
Luke Guinane ◽  
Syed A.M. Tofail ◽  
Micheal D. Scanlon
Keyword(s):  
Self Assembly ◽  
Immiscible Liquid ◽  
Bulk Solution ◽  
Time Resolved ◽  
Force Microscopy ◽  
Atomic Force ◽  
Aggregate Growth ◽  
High Concentrations ◽  
Thermodynamic Processes

<p>Nanostructures that are inaccessible through spontaneous thermodynamic processes may be formed by supramolecular self-assembly under kinetic control. In the past decade, the dynamics of pathway complexity in self-assembly have been elucidated through kinetic models based on aggregate growth by sequential monomer association and dissociation. Immiscible liquid|liquid interfaces are an attractive platform to develop well-ordered self-assembled nanostructures, unattainable in bulk solution, due to the templating interaction of the interface with adsorbed molecules. Here, we report time-resolved <i>in situ</i> UV/vis spectroscopic observations of the self-assembly of zinc(II) meso-tetrakis(4-carboxyphenyl)porphyrin (ZnTPPc) at an immiscible aqueous|organic interface. We show that the kinetically favoured metastable J-type nanostructures form quickly, but then transform into stable thermodynamically favoured H-type nanostructures. Numerical modelling revealed two parallel and competing cooperative pathways leading to the different porphyrin nanostructures. These insights demonstrate that pathway complexity is not unique to self-assembly processes in bulk solution, and equally valid for interfacial self-assembly. Subsequently, the interfacial electrostatic environment was tuned using a kosmotropic anion (citrate) in order to control the influence the pathway selection. At high concentrations, interfacial nanostructure formation was forced completely down the kinetically favoured pathway and only J-type nanostructures were obtained. Furthermore, we found by atomic force microscopy (AFM) and scanning electron microscopy (SEM) that the J- and H-type nanostructures obtained at low and high citric acid concentrations, respectively, are morphologically distinct, which illustrates the pathway-dependent material properties.</p>

Identification of a Novel Gene SRG4 Expressed at Specific Stages of Mouse Spermatogenesis

2004 ◽  
Vol 36 (5) ◽  
pp. 351-359 ◽  
Author(s):  
Xiao-Wei Xing ◽  
Lu-Yun Li ◽  
Gang Liu ◽  
Jun-Jiang Fu ◽  
Xiao-Jun Tan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Mouse Testis ◽  
Amino Acid Residues ◽  
Complex Process ◽  
Testis Cdna Library ◽  
New Gene ◽  
Testis Cdna ◽  
Gene 4

Abstract Spermatogenesis is a complex process. Two spermatocytes expression sequence tags (ESTs) BG101130 and BG100990 were found. Their putative amino acid sequences have high homology with rat Spag4 (sperm antigen 4). By electrical hybridization, a novel cDNA encoding polypeptide of 348 amino acid residues was identified from a mouse testis cDNA library. The new gene was designated as SRG4 (Spermatogenesis related gene 4) (GenBank accession No. AY307077). Results of Northern blot and RTPCR revealed that SRG4 expressed specifically in mouse testis. Changes of SRG4 expression in mouse different development stages were observed by RT-PCR. The SRG4 mRNA was hardly detected in 2 weeks postpartum, and expressed abundantly from 3 weeks later, reaching top lever at 4–5 weeks, while slightly down in aging mouse testis. Results of in situ hybridization showed that SRG4 gene expressed abundantly in spermatocytes, round spermatids. This indicated SRG4 gene may play an important role in mouse meiotic divisions of spermatocytes.

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