Elastin-like polymers (ELPs) are frequently used in a variety of bioengineering applications because of their stimuli-responsive properties. Above their transition temperature, ELPs will adopt different structures that promote intra- and intermolecular hydrophobic contacts to minimize unfavorable interactions with an aqueous environment. We electrochemically characterize the stimuli-responsive behavior of surface-immobilized ELPs corresponding to two proposed states: extended and collapsed. In the extended state the ELPs are more solvated. In the collapsed state, triggered by introducing an environmental stimulus, non-polar intramolecular contacts within ELPs are favored, resulting in quantifiable morphological changes on the surface characterized using electrochemical impedance spectroscopy (EIS). Charge transfer resistance, a component of impedance, was shown to increase after exposing an ELP modified electrode to a high salt concentration environment (3.0 M NaCl). An increase in charge transfer resistance indicates an increase in the insulating layer on the electrode surface consistent with the proposed mechanism of collapse, as the ELPs have undergone morphological changes to hinder the kinetics of the redox couple exchange. Further characterization of the surface-immobilized ELPs showed a reproducible surface modification, as well as reversibility and tunability of the stimuli-response.
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Drug Deliv
December 2025
Biomedical Materials and Devices for Revolutionary Integrative Systems Engineering (BMD-RISE) Research Unit, Faculty of Engineering, Chulalongkorn University, Bangkok, Thailand.
Biopolymers, such as collagens, elastin, silk fibroin, spider silk, fibrin, keratin, and resilin have gained significant interest for their potential biomedical applications due to their biocompatibility, biodegradability, and mechanical properties. This review focuses on the design and integration of biomimetic peptides into these biopolymer platforms to control the release of bioactive molecules, thereby enhancing their functionality for drug delivery, tissue engineering, and regenerative medicine. Elastin-like polypeptides (ELPs) and silk fibroin repeats, for example, demonstrate how engineered peptides can mimic natural protein domains to modulate material properties and drug release profiles.
View Article and Find Full Text PDFLangmuir
January 2025
Department of Chemistry, University of Washington, Seattle, Washington 98195, United States.
Circular dichroism (CD) spectroscopy has emerged as a potent tool for probing chiral small-molecule ligand exchange on natively achiral quantum dots (QDs). In this study, we report a novel approach to identifying QD-biomolecule interactions by inducing chirality in CdS QDs using thermoresponsive elastin-like polypeptides (ELPs) engineered with C-terminal cysteine residues. Our method is based on a versatile two-step ligand exchange process starting from monodisperse oleate-capped QDs in nonpolar media and proceeding through an easily accessed achiral glycine-capped QD intermediate.
View Article and Find Full Text PDFBiomater Adv
December 2024
CBMA (Centre of Molecular and Environmental Biology)/ Aquatic Research Network (ARNET) Associate Laboratory, Department of Biology, University of Minho, Campus of Gualtar, 4710-057 Braga, Portugal; IB-S Institute of Science and Innovation for Sustainability, University of Minho, Campus of Gualtar, 4710-057 Braga, Portugal. Electronic address:
Oncostatin M (OSM) is a pleiotropic cytokine that can significantly enhance wound healing. Here, we report on the use of nanoparticles (NPs) formulated from a genetically engineered A200_hOSM protein polymer, which combines an elastin-like recombinamer (A200) with human OSM (hOSM) in the same molecule, aiming at enhancing wound healing processes. A200_hOSM NPs were obtained by self-assembly and evaluated for their bioactivity in human keratinocytes and fibroblasts.
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
dsm-firmenich Science & Research, Biotechnology, Alexander Fleminglaan 1, Delft 2613 AX, The Netherlands.
The biofabrication of recombinant structural proteins with a range of mechanical or structural features usually relies on the generation of protein libraries displaying variations in terms of amino acid composition, block structure, molecular weight, or physical/chemical cross-linking sites. This approach, while highly successful in generating a wealth of knowledge regarding the links between design features and material properties, has some inherent limitations related to its low throughput. This slows down the pace of the development of recombinant structural proteins.
View Article and Find Full Text PDFBiomacromolecules
January 2025
Department of Chemical Engineering, University of Florida, Gainesville, Florida 32611, United States.
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