The dynamics of elastin-like peptides upon hydrophobic collapse
Elastin-like peptides (ELPs) are artificial polypeptides mimicking the hydrophobic repeat units of the insoluble 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 makes them an intriguing tool for advanced biomaterials, protein purification and drug delivery. In addition, it is widely accepted that 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. 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) and QENS (IN16B, IN5) and complementary techniques. 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 biomedicine.
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MATSARSKAIA Olga; v; HAERTLEIN Michael; KOZA Michael Marek; MOROZOVA Tatiana; PORCAR Lionel; ROOSEN RUNGE Felix; SEYDEL Tilo; Sarah Waldie and WEHBE Zeina. (2021). The dynamics of elastin-like peptides upon hydrophobic collapse. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-916
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