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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The nature of protein interactions governing globular protein-polymer block copolymer self-assembly.
Christopher N. Lam,Minkyu Kim,Carla S. Thomas,Dongsook Chang,Gabriel E. Sanoja,Chimdimma U. Okwara,Bradley D. Olsen +6 more
TL;DR: Measurements of protein/polymer miscibility, second virial coefficients, and zeta potential show that these coarse-grained interactions are similar between mCherry and EGFP, indicating that coarse- grained interactions largely capture the relevant physics for soluble, monomeric globular protein-polymer conjugate self-assembly.
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Recent and prominent examples of nano- and microarchitectures as hemoglobin-based oxygen carriers.
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Topological Effects on Globular Protein‐ELP Fusion Block Copolymer Self‐Assembly
Guokui Qin,Matthew J. Glassman,Christopher N. Lam,Dongsook Chang,Eric Schaible,Alexander Hexemer,Bradley D. Olsen +6 more
TL;DR: In this article, the phase behavior of two mCherry-ELP fusions was investigated to compare linear and bola fusion self-assembly both in diluted and concentrated aqueous solution.
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Highly Active Biocatalytic Coatings from Protein-Polymer Diblock Copolymers.
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Polymer Directed Protein Assemblies
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