Inverse gamma-Turn-Inspired Peptide: Synthesis and Analysis of Segetalin A Indole Hemiaminal

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 the aldehyde and the imine by virtue of the higher reactivity of th...

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Bibliographic Details
Published inEuropean journal of organic chemistry Vol. 2015; no. 34; pp. 7443 - 7448
Main Authors Lamping, Matthias, Enck, Sebastian, Geyer, Armin
Format Journal Article
LanguageEnglish
Published WEINHEIM Wiley 01.12.2015
Subjects
Chemistry
Chemistry, Organic
Physical Sciences
Science & Technology
Peptides
Cyclization
Nitrogen heterocycles
Aldehydes
Macrocycles
CYCLIC HEXAPEPTIDE
BETA
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Summary: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 the aldehyde and the 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. Herein, we analyzed this uncommon hemiaminal that shows that the biosynthesis of cyclic peptides is not necessarily based on linear precursor peptides with a high inherent macrolactamization tendency.
ISSN:1434-193X
1099-0690
DOI:10.1002/ejoc.201501179