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Structural and Dynamical Properties of Elastin-Like Peptides near their Lower Critical Solution Temperature
Open accessPreprint — published as 10.1021/acs.biomac.3c00124
Abstract
Elastin-like peptides (ELPs) are artificially derived intrinsically disordered proteins (IDPs) mimicking the hydrophobic repeat unit in the protein elastin. ELPs are characterized by a lower critical solution temperature (LCST) in aqueous media. Here, we investigate the sequence GVG(VPGVG) 3 over a wide range of temperatures (below, around, and above the LCST) and peptide concentrations employing all-atom molecular dynamics simulations, where we focus on the role of intra- and inter-peptide interactions. We begin by investigating the structural properties of a single peptide that demonstrates a hydrophobic collapse with temperature, albeit moderate, as the sequence length is short. We observe a change in the interaction between two peptides from repulsive to attractive with temperature by evaluating the potential of mean force, indicating an LCST-like behaviour. Next, we explore dynamical and structural properties of peptides in multi-chain systems. We report the formation of dynamical aggregates with coil-like conformation, in which Val central residues play an important role. Moreover, the lifetime of contacts between chains strongly depends on the temperature and can be described by a power-law decay that is consistent with the LCST-like behaviour. Finally, the peptide translational and internal motion are slowed down by an increase in the peptide concentration and temperature.
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Metadata
- Authors
- Morozova, T. I., García, N. A., Matsarskaia, O., Roosen-Runge, F., & Barrat, J.-L.
- Affiliations
- Institut Laue-Langevin (FR)
- Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Morozova, Tatiana I.
- Venue
- Biomacromolecules
- Publisher
- openRxiv
- Published
- 2022-09-26
- Volume
- 24
- Issue
- 4
- Pages
- 1912-1923
- ISSN
- 1525-7797 (ISSN-L)
- OpenAlex
- W4323322124
- Cited by
- 11
- References
- 2
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 4 · 2023: 1
- FWCI
- 0.98
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Biomacromolecules (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Centre National de la Recherche Scientifique
- Grand Équipement National De Calcul Intensif
- Université de Poitiers (PICT 2019-02257)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Advanced Physical and Chemical Molecular Interactions
- Keywords
- elastin-like peptides, lower critical solution temperature, intrinsically disordered proteins, hydrophobic collapse, potential of mean force, peptide aggregation, power-law decay, temperature dependence, peptide concentration dependence
- MeSH terms
- Cold Temperature, Elastin, Peptides, Temperature, Molecular Dynamics Simulation
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