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- Title
Probing Peptidylprolyl Bond cis/trans Status Using Distal <sup>19</sup>F NMR Reporters.
- Authors
Killoran, Patrick M.; Hanson, George S. M.; Verhoork, Sanne J. M.; Smith, Madeleine; Del Gobbo, Davide; Lu-Yun Lian; Coxon, Christopher R.
- Abstract
A method for measuring peptidylprolyl bond cistrans conformational status in peptide models is described, using 4-fluorophenylalanine (4FPhe) as a distal reporter for 19F NMR. The %cis-Pro population was measured for peptides of the general structure Ac-X-Pro-Z-Ala-Ala-4FPhe (X and Z are proteinogenic amino acids) at pH 7.4, and provided conformational populations consistent with literature values obtained by more complex methods. This approach was applied to probe the prolyl bond status in pentapeptide models of the intrinsically disordered C-terminal region of α-synuclein, which mirrored the preferences in the Ac-X-Pro-Z-Ala-4FPhe models. Advantageously, the 19F reporter group does not need to be adjacent to or attached to proline to provide quantifiable signals and distal 4-fluorophenylalanines can be placed so as not to influence prolyl bond conformation. Finally, we demonstrated that the prolyl bond status is not significantly affected by pH when there are ionisable amino acid residues at the carboxyl side of proline, which makes 19F NMR an invaluable tool with which to study proline isomerism at a range of pHs and in different solvents and buffers.
- Subjects
AMINO acid residues; AMINO acids; PEPTIDES; ALPHA-synuclein; PROLINE
- Publication
Chemistry - A European Journal, 2023, Vol 29, Issue 16, p1
- ISSN
0947-6539
- Publication type
Article
- DOI
10.1002/chem.202203017