| Literature DB >> 30221816 |
Zhanna Evgrafova1, Bruno Voigt2, Monika Baumann2, Madlen Stephani2, Wolfgang H Binder1, Jochen Balbach2.
Abstract
Covalent conjugates between a synthetic polymer and a peptide hormone were used to probe the molecular extension of these macromolecules and how the polymer modifies the fibril formation of the hormone. NMR spectroscopy of 15 N labeled parathyroid hormone (PTH) was employed to visualize the conformation of the conjugated synthetic polymer, triggered by small temperature changes via its lower critical solution temperature. A shroud-like polymer conformation dominated the molecular architecture of the conjugated chimeras. PTH readily forms amyloid fibrils, which is probably the physiological storage form of the hormone. The polyacrylate based polymers stimulated the nucleation processes of the peptide.Entities:
Keywords: NMR spectroscopy; macromolecular conformation; parathyroid hormone; protein fibrils; thermo-responsive polymer
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Year: 2018 PMID: 30221816 DOI: 10.1002/cphc.201800867
Source DB: PubMed Journal: Chemphyschem ISSN: 1439-4235 Impact factor: 3.102