ArticleBiomacromolecules2013
Switchable elastin-like polypeptides that respond to chemical inducers of dimerization.
Article in Biomacromolecules, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Lipidation alters the phase-separation of resilin-like polypeptides.Soft matter · 2024Article
- Hydra-Elastin-like Polypeptides Increase Rapamycin Potency When Targeting Cell Surface GRP78.Biomacromolecules · 2022Article
- Purification of a Hydrophobic Elastin-Like Protein Toward Scale-Suitable Production of Biomaterials.Frontiers in bioengineering and biotechnology · 2022Article
- Tuning the Properties of Protein-Based Polymers Using High-Performance Orthogonal Translation Systems for the Incorporation of Aromatic Non-Canonical Amino Acids.Frontiers in bioengineering and biotechnology · 2022Article
- Simple Regulation of the Self-Assembling Ability by Multimerization of Elastin-Derived Peptide (FPGVG)ACS omega · 2021Article
- Adaptable antibody Nanoworms designed for non-Hodgkin lymphoma.Biomaterials · 2020Article
- Nanotoxicology of an Elastin-like Polypeptide Rapamycin Formulation for Breast Cancer.Biomacromolecules · 2020Article
- A novel elastin-like polypeptide drug carrier for cyclosporine A improves tear flow in a mouse model of Sjögren's syndrome.Journal of controlled release : official journal of the Controlled Release Society · 2018Article
- Effects of Doxorubicin on the Liquid-Liquid Phase Change Properties of Elastin-Like Polypeptides.Biophysical journal · 2018Article
- Copper mediated amyloid-β binding to Transthyretin.Scientific reports · 2018Article
- Bifunctional Elastin-like Polypeptide Nanoparticles Bind Rapamycin and Integrins and Suppress Tumor Growth in Vivo.Bioconjugate chemistry · 2017Article
- Elastin-like polypeptide switches: A design strategy to detect multimeric proteins.Protein science : a publication of the Protein Society · 2017Article
- Berunda Polypeptides: Multi-Headed Fusion Proteins Promote Subcutaneous Administration of Rapamycin to Breast CancerTheranostics · 2017Article
- A thermo-responsive protein treatment for dry eyes.Journal of controlled release : official journal of the Controlled Release Society · 2015Article
- Triggered sorting and co-assembly of genetically engineered protein microdomains in the cytoplasm.Advanced materials (Deerfield Beach, Fla.) · 2014Article
- Genetically engineered nanocarriers for drug delivery.International journal of nanomedicine · 2014Review
- A rapamycin-binding protein polymer nanoparticle shows potent therapeutic activity in suppressing autoimmune dacryoadenitis in a mouse model of Sjögren's syndrome.Journal of controlled release : official journal of the Controlled Release Society · 2013Article
- Elastin-based protein polymer nanoparticles carrying drug at both corona and core suppress tumor growth in vivo.Journal of controlled release : official journal of the Controlled Release Society · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Elastin-like polypeptides (ELPs) are protein polymers that reversibly phase separate in response to increased temperature, pressure, concentration, ionic strength, and molecular weight. If it were possible to engineer their phase separation to respond to specific molecular substrates, ELP fusion proteins might be engineered as biosensors, smart biomaterials, diagnostic imaging agents, and targeted therapies. What has been lacking is a strategy to design ELPs to respond to specific substrates. To address this deficiency, we report that ELP fusion proteins phase separate in response to chemical inducers of dimerization (CID). The rationale is that ELP phase separation depends on molecular weight, concentration, and local hydrophobicity; therefore, processes that affect these properties, including noncovalent dimerization, can be tuned to produce isothermal phase separation. To test this hypothesis, constructs were evaluated consisting of an immunophilin: human FK-506 binding protein 12 (FKBP) attached to an ELP. Under stoichiometric binding of a CID, the fusion protein homodimerizes and triggers phase separation. This dimerization is reversible upon saturation with excess CID or competitive binding of a small lipophilic macrolide to FKBP. By modulating the ELP molecular weight, phase separation was tuned for isothermal response to CID at physiological ionic strength and temperature (37 °C). To interpret the relationship between transition temperature and equilibrium binding constants, an empirical mathematical model was employed. To the best of our knowledge, this report is the first demonstration of reversible ELP switching in response to controlled dimerization. Due to its simplicity, this strategy may be useful to design ELP fusion proteins that respond to specific dimeric biological entities.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.