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Reversible Boronic Ester Formation of Ribopyranosylated Glycopeptides
Author(s) -
Kirschner Romina A.,
Geyer Armin
Publication year - 2016
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201601240
Subject(s) - chemistry , amino acid , boronic acid , pyrene , oligopeptide , glycosidic bond , peptide , thiol , glycopeptide , side chain , combinatorial chemistry , stereochemistry , organic chemistry , biochemistry , enzyme , antibiotics , polymer
Six natural amino acids bearing hydroxy or thiol groups are transformed into N ‐Fmoc and O ‐acetyl protected ribopyranosylated amino acids (Raa) for further use in solid‐phase peptide synthesis (SPPS). Although the different O ‐ and S ‐glycosidic bonds influence the 1 C 4 / 4 C 1 equilibrium of the ribopyranosyl side chain significantly, the oligopeptides containing Raa are capable of spontaneous boronic ester formation. Ligation of model peptides with pyrene boronic acid and competition experiments between different peptides are monitored by NMR spectroscopy. In addition to boronic ester formation, we further propose ribopyranosylated peptides with adjustable orientation of the trihydroxy ax‐eq‐ax disposition for other applications.