ArticleBiomacromolecules2013
Predicting transition temperatures of elastin-like polypeptide fusion proteins.
Article in Biomacromolecules, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 132 citations in OpenAlex.
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- Intracellular GRP78-Directed Delivery of Rapamycin by Biomolecular Condensates of Hydra-Elastin-like Polypeptides.Biomacromolecules · 2026Article
- Using cyclic voltammetry to probe the conformational transition of short elastin-like peptides.Communications chemistry · 2026Article
- Rational design and preclinical evaluation of elastin-like polypeptide micelle nanoparticles for drug delivery.Frontiers in bioengineering and biotechnology · 2026Review
- An Elastin-like Polymer Targeting Vascular Endothelial Growth Factor Receptor-1 Reduces Survival in Serum-Starved Endothelial Cells.Biochemical engineering journal · 2026Article
- Controlling Release Kinetics of an Adjuvant from a Depot Improves the Efficacy of Local Immunotherapy in Metastatic Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A Thermogenetic Tool Employing Elastin-like Polypeptides for Controlling Programmed Cell Death.ACS nano · 2025Article
- Protein Translocation Control inBiomolecules · 2025Article
- Functional Design and Biophysical Characterization of Analyte-Responsive Polymers.Biomacromolecules · 2025Article
- Architectural control of rod-coil block polypeptide thermoresponsive self-assemblyJournal of materials chemistry. B · 2025Article
- Genetically-Encoded Phase Separation Sensors Enable High-Fidelity Live-Cell Probing of Biomolecular Condensates.ACS sensors · 2025Article
- Synthetic biomolecular condensates enhance translation from a target mRNA in living cells.Nature chemistry · 2025Article
- Reversible light-responsive protein hydrogel for on-demand cell encapsulation and release.Acta biomaterialia · 2025Article
- A tunable affinity fusion tag for protein self-assembly.bioRxiv : the preprint server for biology · 2025Article
- A thermo-sensitive peptide hydrogel loaded with paclitaxel and antimony nanosheets for synergistic photothermal-chemotherapeutic treatment of breast cancer.Frontiers in pharmacology · 2025Article
- Genetically-encoded phase separation sensors for intracellular probing of biomolecular condensates.bioRxiv : the preprint server for biology · 2024Article
- Understanding the Phase Behavior of a Multistimuli-Responsive Elastin-like Polymer: Insights from Dynamic Light Scattering Analysis.The journal of physical chemistry. B · 2024Article
- Synthetic intrinsically disordered protein fusion tags that enhance protein solubility.Nature communications · 2024Article
- Isolation of nucleic acids using liquid-liquid phase separation of pH-sensitive elastin-like polypeptides.Scientific reports · 2024Article
- Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Elastin-like polypeptides (ELPs) are thermally sensitive peptide polymers that undergo thermally triggered phase separation and this behavior is imparted to soluble proteins when they are fused to an ELP. The transition temperature of the ELP fusion protein is observed to be different than that of a free ELP, indicating that the surface properties of the fused protein modulate the thermal behavior of ELPs. Understanding this effect is important for the rational design of applications that exploit the phase transition behavior of ELP fusion proteins. We had previously developed a biophysical model that explained the effect of hydrophobic proteins on depressing the transition temperature of ELP fusion proteins relative to free ELP. Here, we extend the model to elucidate the effect of hydrophilic proteins on the thermal behavior of ELP fusion proteins. A linear correlation was found between overall residue composition of accessible protein surface weighted by a characteristic transition temperature for each residue and the difference in transition temperatures between the ELP protein fusion and the corresponding free ELP. In breaking down the contribution of residues to polar, nonpolar, and charged, the model revealed that charged residues are the most important parameter in altering the transition temperature of an ELP fusion relative to the free ELP.
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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.