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First Total Synthesis of Hormaomycin, a Naturally Occurring Depsipeptide with Interesting Biological Activities
Author(s) -
Zlatopolskiy Boris D.,
de Meijere Armin
Publication year - 2004
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200400249
Subject(s) - depsipeptide , residue (chemistry) , natural product , stereochemistry , isoleucine , chemistry , threonine , alanine , amino acid residue , biological activity , amino acid , serine , biochemistry , peptide sequence , leucine , in vitro , gene , enzyme
Some unique features were disclosed during the structure elucidation of the cyclic depsipeptide hormaomycin ( 1 ), first isolated in 1989 from a Streptomyces griseoflavus strain and found to have quite an interesting spectrum of biological activities. Besides one residue of the proteinogenic amino acid isoleucine [( S )‐Ile], it contains two units of 3‐methylphenylalanine [(βMe)Phe], one of (2 R )‐ allo ‐threonine [ a ‐Thr] as well as two moieties of 3‐( trans ‐2‐nitrocyclopropyl)alanine [(3‐Ncp)Ala] and one of 4‐( Z )‐propenylproline [(4‐PE)Pro]. The latter two have never been found in any natural product before. The side chain of 1 is terminated with the residue of 5‐chloro‐1‐hydroxypyrrole‐2‐carboxylic acid [Chpca]. This first synthetic access to hormaomycin 1 will make it possible to prepare structural analogues of this interesting natural depsipeptide in order to elucidate structure–activity relationships and the biologically active minimal unit.