Thermally-responsive, short elastin-like peptides (ELPs) of sequence VPGVG (V, P and G represent valine, proline and glycine respectively), bearing different N-terminal functional groups (amino-, N-acetyl and thiol) and a non-ionisable C-terminal group, were prepared by solid phase synthesis. The conformation and aggregation properties of the ELPs were studied in different pH aqueous buffer solutions using UV-vis spectroscopy and circular dichroism (CD). The thiol-capped ELPs were used to prepare functionalized gold nanoparticles (GNPs), which were found to undergo thermally-triggered reversible aggregation at 40 °C. The peptide conformation and nanoparticle aggregation behaviour of the ELP-GNPs in aqueous solution were investigated by transmission electron microscopy (TEM), circular dichroism (CD) and UV-vis spectroscopy. It was found that the ELP-GNP conjugates were capable of reversible, thermally triggered aggregation at near-physiological temperatures (transition temperature of 40 °C at pH = 7.4), opening up applications in photothermal cancer therapy and diagnosis.
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http://dx.doi.org/10.1039/c8tb01827h | DOI Listing |
J Mater Chem B
January 2025
Shanghai Key Laboratory of Chemical Biology, School of Pharmacy, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, P. R. China.
Intracellular macromolecules have the ability to form membraneless compartments, such as vacuoles and hollow condensates, through liquid-liquid phase separation (LLPS) in order to adapt to changes in their environment. The development of artificial non-homogeneous compartments, such as multiphase hollow or multicavity condensates, has gained significant attention due to their potential to uncover the mechanisms underlying the formation of artificial condensates and biomolecular condensates. However, the complexity of design and construction has hindered progress, particularly in creating dynamic non-homogeneous compartments.
View Article and Find Full Text PDFACS 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 PDFSoft Matter
January 2025
Department of Chemical Engineering, University of Washington, Seattle, Washington 98195, USA.
High information content building blocks offer a path toward the construction of precision materials by supporting the organization and reconfiguration of organic and inorganic components through engineered functions. Here, we combine thermoresponsiveness with biomimetic mineralization by fusing the Car9 silica-binding dodecapeptide to the C-terminus of the (VPGVG) elastin-like polypeptide (ELP). Using small angle X-ray scattering, we show that the short Car9 cationic block is sufficient to promote the conversion of disordered unimers into 30 nm micelles comprising about 150 proteins, 5 °C above the transition temperature of the ELP.
View Article and Find Full Text PDFJ Phys Chem Lett
October 2024
Laboratoire Interdisciplinaire de Physique, Université Grenoble Alpes-CNRS, 38000 Grenoble, France.
It appeared certain that elastin condensates retain liquid-like properties. However, a recent experimental study demonstrated that their aggregate states might depend on the length of hydrophobic domains. To gain microscopic insight into this behavior, we employ atomistic modeling to assess the conformational properties of hydrophobic elastin-like polypeptides (ELPs).
View Article and Find Full Text PDFBiomacromolecules
November 2024
Department of Chemistry, Faculty and Graduate School of Science, Kyushu University, Fukuoka 819-0395, Japan.
Elastin-like peptides (ELPs) exhibit lower critical solution temperature (LCST)-type behavior, being soluble at low temperatures and insoluble at high temperatures. While the properties of linear, long-chain ELPs are well-studied, short-chain ELPs, especially those with branched architectures, have been less explored. Herein, to obtain further insights into multimeric short ELPs, we investigated the temperature-responsive properties of branched molecules composed of a repeating pentapeptide unit of short ELPs, Phe-Pro-Gly-Val-Gly, as side components and oligo(Glu) as a backbone structure.
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