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Inverse γ‐Turn‐Inspired Peptide: Synthesis and Analysis of Segetalin A Indole Hemiaminal (Eur. J. Org. Chem. 34/2015)
Author(s) -
Lamping Matthias,
Enck Sebastian,
Geyer Armin
Publication year - 2015
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201590097
Subject(s) - chemistry , hemiaminal , aldehyde , peptide , imine , aminal , indole test , stereochemistry , peptide bond , cyclic peptide , combinatorial chemistry , organic chemistry , catalysis , biochemistry
The cover picture shows the reversible cyclization of a peptide aldehyde, which is based on the cyclic hexapeptide Segetalin A. The traffic light symbolizes the formation of the species involved in this reaction. The substitution of a peptide bond for an imine transforms the irreversible macrocyclization of peptides into a reversible process. The inherent cyclization tendency of a linear peptide is then analyzable through the equilibrium between aldehyde and imine by virtue of the higher reactivity of the corresponding linear peptide aldehyde. The tryptophan side chain of Segetalin A aldehyde forms a 12‐membered cyclic indole hemiaminal instead of the 18‐membered macrocyclic imine expected. In this article on 7443 ff , A. Geyer et al. analyze this uncommon hemiaminal, which shows that the biosynthesis of cyclic peptides is not necessarily based on linear precursor peptides with a high inherent macrolactamization tendency.