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Structure Elucidation of the Peptide Antibiotics Herbicolin A and B
Author(s) -
Aydin Mitat,
Lucht Norbert,
König Wilfried A.,
Lupp Rudolf,
Jung Günther,
Winkelmann Günther
Publication year - 1985
Publication title -
liebigs annalen der chemie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 0170-2041
DOI - 10.1002/jlac.198519851117
Subject(s) - chemistry , glycosidic bond , residue (chemistry) , moiety , stereochemistry , peptide , peptide bond , antibiotics , lactone , ring (chemistry) , biochemistry , organic chemistry , enzyme
The structures of the amphiphilic peptide antibiotics herbicolin A and B were determined by application of physical methods, chemical degradation, and partial syntheses. Herbicolin B is a lipodepsinonapeptide with the sequence DH‐Abu‐L‐Thr‐D‐aThr‐D‐Leu‐Gly‐D‐Gln‐Gly‐ N ‐Me‐L‐aThr‐L‐Arg (DH‐Abu = 2,3‐dehydro‐α‐aminobutyric acid). The C‐terminal Arg residue forms a lactone ring with the hydroxy group of L‐Thr, while the N‐terminus is acylated by an ( R )‐3‐hydroxytetradecanoic acid residue. The main component herbicolin A differs from herbicolin B in an additional D‐glucose moiety linked in an 1‐α‐glycosidic bond to the 3‐hydroxytetradecanoic acid residue. Thus herbicolin A constitutes the first glycolipodepsinonapeptide antibiotic known so far.

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