Water + elastin-like polypeptides (ELPs) exhibit a transition temperature below which the chains transform from collapsed to expanded states, reminiscent of the cold denaturation of proteins. This conformational change coincides with liquid-liquid phase separation. A statistical-thermodynamics theory is used to model the fluid-phase behavior of ELPs in aqueous solution and to extrapolate the behavior at ambient conditions over a range of pressures. At low pressures, closed-loop liquid-liquid equilibrium phase behavior is found, which is consistent with that of other hydrogen-bonding solvent + polymer mixtures. At pressures evocative of deep-sea conditions, liquid-liquid immiscibility bounded by two lower critical solution temperatures (LCSTs) is predicted. As pressure is increased further, the system exhibits two separate regions of closed-loop of liquid-liquid equilibrium (LLE). The observation of bimodal LCSTs and two re-entrant LLE regions herald a new type of binary global phase diagram: Type XII. At high-ELP concentrations the predicted phase diagram resembles a protein pressure denaturation diagram; possible "molten-globule"-like states are observed at low concentration.
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http://dx.doi.org/10.1039/d0cp05013j | DOI Listing |
ACS Omega
November 2024
CBMA (Centre of Molecular and Environmental Biology)/ARNET (Aquatic Research Network) Associate Laboratory, Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal.
Oncostatin M (OSM) and leukemia inhibitory factor (LIF) are pleiotropic cytokines from the interkeukine-6 family, associated with several disorders, and present significant potential in biomedicine. However, their therapeutic use is highly constrained by factors such as short circulating half-life and narrow therapeutic window. The conjugation of cytokines with elastin-like recombinamers (ELR) holds the potential to circumvent these limitations due to the ability of self-assembling upon a thermal stimulus, remarkable biocompatibility, and ease of processing.
View Article and Find Full Text PDFNanomaterials (Basel)
November 2024
Department of Pharmaceutical Sciences, North Carolina Central University, Durham, NC 27707, USA.
This paper reports the development of a highly crosslinked hyper-branched polyglycerol (HPG) polymer bound to elastin-like proteins (ELPs) to create a membrane that undergoes a distinct closed-to-open permeation transition at 32 °C. The crosslinked HPG forms a robust, mesoporous structure (150-300 nm pores), suitable for selective filtration. The membranes were characterized by FTIR, UV-visible spectroscopy, SEM, and AFM, revealing their structural and morphological properties.
View Article and Find Full Text PDFBioconjug Chem
December 2024
ICGM, University Montpellier, CNRS, ENSCM, Montpellier 34293, France.
Biomacromolecules
September 2024
Department of Chemical Engineering, University of Florida, 1006 Center Drive, Gainesville, Florida 32611, United States.
We present a straightforward strategy for constructing giant, multicompartmentalized vesicles using recombinant fusion proteins. Our method leverages the self-assembly of globule-zipper-elastin-like polypeptide fusion protein complexes in aqueous conditions, eliminating the need for organic solvents and chemical conjugation. By employing the thin-film rehydration method, we have successfully encapsulated a diverse range of bioactive macromolecules and engineered organelle-like compartments─ranging from soluble proteins and coacervate droplets to vesicles─within these protein-assembled giant vesicles.
View Article and Find Full Text PDFACS Appl Bio Mater
July 2024
Key Lab of Molecular Biophysics of Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, 1037 Luoyu Road, Wuhan 430074, China.
There is an emerging strong demand for smart environmentally responsive protein-based biomaterials with improved adhesion properties, especially underwater adhesion for potential environmental and medical applications. Based on the fusion of elastin-like polypeptides (ELPs), SpyCatcher and SpyTag modules, biosynthetic barnacle-derived protein was genetically engineered and self-assembled with an enhanced adhesion ability and temperature response. The water resistance ability of the synthetic protein biopolymer with a network structure increased to 98.
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