Thermal compaction of disordered and elastin-like polypeptides: a temperature-dependent, sequence-specific coarse-grained simulation model
| Autor: | Joachim Dzubiella, Upayan Baul, Michael Bley |
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| Rok vydání: | 2020 |
| Předmět: |
Work (thermodynamics)
Materials science Polymers and Plastics FOS: Physical sciences Bioengineering Sequence (biology) 02 engineering and technology Condensed Matter - Soft Condensed Matter 010402 general chemistry 01 natural sciences Biomaterials Hydrophobic effect Materials Chemistry Transition Temperature Physics - Biological Physics Solubility chemistry.chemical_classification Cloud point Quantitative Biology::Biomolecules Coacervate Transition temperature Temperature Polymer 021001 nanoscience & nanotechnology 0104 chemical sciences Elastin chemistry Chemical physics Biological Physics (physics.bio-ph) Soft Condensed Matter (cond-mat.soft) 0210 nano-technology Peptides Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Biomacromolecules |
| DOI: | 10.48550/arxiv.2007.11387 |
| Popis: | Elastin-like polypeptides (ELPs) undergo a sharp solubility transition from low temperature solvated phases to coacervates at elevated temperatures, driven by the increased strength of hydrophobic interactions at higher temperatures. The transition temperature, or 'cloud point', critically depends on sequence composition, sequence length, and concentration of the ELPs. In this work, we present a temperature-dependent, implicit solvent, sequence-specific coarse-grained (CG) simulation model that reproduces the transition temperatures as a function of sequence length and guest residue identity of various experimentally probed ELPs to appreciable accuracy. Our model builds upon the self-organized polymer model introduced recently for intrinsically disordered polypeptides (SOP-IDP), and introduces a semi-empirical functional form for the temperature-dependence of hydrophobic interactions. In addition to the fine performance for various ELPs, we demonstrate the ability of our model to capture the thermal compactions in dominantly hydrophobic intrinsically disordered polypeptides (IDPs), consistent with experimental scattering data. With the high computational efficiency afforded by the CG representation, we envisage that the model will be ideally suited for simulations of large-scale structures such as ELP networks and hydrogels, as well as agglomerates of IDPs. |
| Databáze: | OpenAIRE |
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