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Probing Polymer Chain Conformation and Fibril Formation of Peptide Conjugates
Author(s) -
Evgrafova Zhanna,
Voigt Bruno,
Baumann Monika,
Stephani Madlen,
Binder Wolfgang H.,
Balbach Jochen
Publication year - 2019
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201800867
Subject(s) - polymer , conjugated system , fibril , macromolecule , chemistry , peptide , dendrimer , conjugate , covalent bond , polymer chemistry , biophysics , organic chemistry , biochemistry , mathematical analysis , mathematics , biology
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.