Open AccessJournal Article
Phase Transitions in Concentrated Solution Self-Assembly of Globular Protein-Polymer Block Copolymers
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The phase behavior of mCherry-b-PNIPAM (mChP) block copolymers with four different PNIPAM coil fractions was investigated in concentrated aqueous solution as a function of both concentration and temperature.Abstract:
The phase behaviour of mCherry-b-PNIPAM (mChP) block copolymers with four different PNIPAM coil fractions is investigated in concentrated aqueous solution as a function of both concentration and temperature, demonstrating both order–order transitions (OOTs) and order–disorder transitions (ODTs) in globular protein–polymer block copolymers. Independent of coil volume fraction from 0.25 to 0.70, the temperature–concentration phase diagrams share several common features. At low concentrations, mCherry-b-PNIPAM forms a homogeneous disordered phase, and macrophase separation into an ordered conjugate-rich phase and a solvent-rich phase is observed at temperatures above the PNIPAM thermoresponsive transition temperature. mChP solutions are also observed to undergo a low-temperature ODT driven by increasing concentration. The order–disorder transition concentration (ODTC) behaviour of mChP is minimized for symmetric conjugates, suggesting that repulsive solvent-mediated protein–polymer interactions provide a driving force for self-assembly. Both coil fraction and solvent selectivity have large effects on the morphologies formed—disordered micelles, hexagonally packed cylinders, lamellae, and perforated lamellae are identified with the combination of small-angle X-ray scattering (SAXS), depolarized light scattering (DPLS), turbidimetry, and differential scanning calorimetry (DSC). An OOT is observed upon increasing temperature for three of the studied coil fractions at concentrations of 40–50 wt% due to changing solvent selectivity. SANS contrast-matching experiments show that water is weakly selective for PNIPAM at low temperatures and strongly selective for mCherry at high temperatures.read more
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Effect of small molecule osmolytes on the self-assembly and functionality of globular protein-polymer diblock copolymers.
TL;DR: The results suggest that hydrogen bond replacement is responsible for the retention of protein function but suppression or enhancement of thermal motion based on the glass transition of the osmolyte primarily determines thermal stability.
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Block copolymers for protein ordering
TL;DR: A review of block copolymer self-assembly can be found in this article, where the authors focus on how the systems have been characterized and focus on the inherent difficulty of such systems.
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Self‐Assembly of Differently Shaped Protein–Polymer Conjugates through Modification of the Bioconjugation Site
Aaron Huang,Bradley D. Olsen +1 more
TL;DR: Self-assembly of protein-polymer block copolymers is an attractive route for preparing biocatalytic materials, and four different conjugation sites are selected on the surface of the model globular protein mCherry at residues 3, 108, 131, and 222 to alter the colloidal shape of the bioconjugate.
Journal ArticleDOI
The effect of THF and the chelating modifier DTHFP on the copolymerisation of β-myrcene and styrene: kinetics, microstructures, morphologies, and mechanical properties
Dominik A. H. Fuchs,Hanna Hübner,Tobias Kraus,Bart-Jan Niebuur,Markus Gallei,Holger Frey,Axel H. E. Müller +6 more
TL;DR: In this paper, the statistical anionic copolymerisation of the biobased monomer β-myrcene with styrene in cyclohexane was investigated via in situ near-infrared (NIR) spectroscopy, focusing on the influence of the modifiers (i.e., Lewis bases) tetrahydrofuran (THF) and 2,2-di(2-tetrahydrafuryl)propane (DTHFP) on the reactivity ratios.
Journal ArticleDOI
Kinetic Effects on Self‐Assembly and Function of Protein–Polymer Bioconjugates in Thin Films Prepared by Flow Coating
TL;DR: Fluorescence emission spectra of mCherry in films prepared at <25% relative humidity shows a small shift suggesting that proteins are more perturbed at low humidity than high humidity or the solution state.
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