Structural and Dynamical Properties of Elastin-Like Peptides near Their Lower Critical Solution Temperature
(2023) In Biomacromolecules 24(4). p.1912-1923- 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 interpeptide interactions. We begin by investigating the structural properties of a single peptide that demonstrates a hydrophobic collapse with temperature, albeit moderate, because the sequence length is short. We observe a change in the interaction... (More)
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 interpeptide interactions. We begin by investigating the structural properties of a single peptide that demonstrates a hydrophobic collapse with temperature, albeit moderate, because 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 behavior. Next, we explore dynamical and structural properties of peptides in multichain systems. We report the formation of dynamical aggregates with coil-like conformation, in which valine 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 behavior. Finally, the peptide translational and internal motion are slowed by an increase in the peptide concentration and temperature.
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- author
- Morozova, Tatiana I. ; García, Nicolás A. ; Matsarskaia, Olga ; Roosen-Runge, Felix LU and Barrat, Jean Louis
- publishing date
- 2023-04-10
- type
- Contribution to journal
- publication status
- published
- in
- Biomacromolecules
- volume
- 24
- issue
- 4
- pages
- 12 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:36877869
- scopus:85149788120
- ISSN
- 1525-7797
- DOI
- 10.1021/acs.biomac.3c00124
- language
- English
- LU publication?
- no
- id
- d5d1813c-9676-433f-9676-779ed98f92ef
- date added to LUP
- 2023-08-14 10:23:51
- date last changed
- 2024-04-20 00:30:47
@article{d5d1813c-9676-433f-9676-779ed98f92ef,
abstract = {{<p>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)<sub>3</sub> 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 interpeptide interactions. We begin by investigating the structural properties of a single peptide that demonstrates a hydrophobic collapse with temperature, albeit moderate, because 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 behavior. Next, we explore dynamical and structural properties of peptides in multichain systems. We report the formation of dynamical aggregates with coil-like conformation, in which valine 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 behavior. Finally, the peptide translational and internal motion are slowed by an increase in the peptide concentration and temperature.</p>}},
author = {{Morozova, Tatiana I. and García, Nicolás A. and Matsarskaia, Olga and Roosen-Runge, Felix and Barrat, Jean Louis}},
issn = {{1525-7797}},
language = {{eng}},
month = {{04}},
number = {{4}},
pages = {{1912--1923}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Biomacromolecules}},
title = {{Structural and Dynamical Properties of Elastin-Like Peptides near Their Lower Critical Solution Temperature}},
url = {{http://dx.doi.org/10.1021/acs.biomac.3c00124}},
doi = {{10.1021/acs.biomac.3c00124}},
volume = {{24}},
year = {{2023}},
}