Abstract
Macrocyclic peptides are an important class of bioactive substances. When inserting an aromatic foldamer segment in a macrocyclic peptide, the strong folding propensity of the former may influence the conformation and alter the properties of the latter. Such an insertion is relevant because some foldamer-peptide hybrids have recently been shown to be tolerated by the ribosome, prior to forming macrocycles, and can thus be produced using an in vitro translation system. We have investigated the interplay of peptide and foldamer conformations in such hybrid macrocycles. We show that foldamer helical folding always prevails and stands as a viable means to stretch, i.e. unfold, peptides in a solvent dependent manner. Conversely, the peptide systematically has a reciprocal influence and gives rise to strong foldamer helix handedness bias as well as foldamer helix stabilisation. The hybrid macrocycles also show resistance towards proteolytic degradation.
Dokumententyp: | Zeitschriftenartikel |
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Fakultät: | Chemie und Pharmazie > Department für Pharmazie - Zentrum für Pharmaforschung |
Fakultätsübergreifende Einrichtungen: | Center for Integrated Protein Science Munich (CIPSM) |
Themengebiete: | 500 Naturwissenschaften und Mathematik > 540 Chemie |
ISSN: | 2041-6520 |
Sprache: | Englisch |
Dokumenten ID: | 97685 |
Datum der Veröffentlichung auf Open Access LMU: | 05. Jun. 2023, 15:26 |
Letzte Änderungen: | 17. Okt. 2023, 14:56 |