Structure and dynamics of elastin-like peptides upon hydrophobic collapse
Elastin-like peptides (ELPs) are artificial polypeptides mimicking the hydrophobic repeat units of the protein elastin which provides elasticity to several biological tissues. One of the main features of ELPs is a hydrophobic collapse upon crossing a lower critical solution temperature (LCST), which induces stimulus-response useful for advanced biomaterials, protein purification and drug delivery. In addition, this hydrophobic collapse is key for the elastic properties of elastin. However, a comprehensive structural and dynamic characterization of the collapse process and the final, collapsed state is still missing, and debated in literature. Using fully hydrogenated and partially deuterated ELP molecules, we aim for a comprehensive understanding of the hydrophobic collapse in ELPs by combining structural, dynamical and thermodynamic signatures using SANS (D22), QENS (IN5), complementary techniques and simulations. Crucially, the partial deuteration will allow for elucidation of the dynamic contributions of the peptide backbone and side chains. Our study will provide valuable insights into the molecular nature of the hydrophobic collapse of ELPs and its role in bioapplications.
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The recommended format for citing this dataset in a research publication is in the following format:
ROOSEN RUNGE Felix; KOZA Michael Marek; MATSARSKAIA Olga; MOROZOVA Tatiana; Sarah Waldie and WEHBE Zeina. (2021). Structure and dynamics of elastin-like peptides upon hydrophobic collapse. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-954
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