ANTIFUNGAL CYCLIC PEPTIDES FROM THE TERRESTRIAL BLUE-GREEN ALGA Anabaena laxa II. STRUCTURES OF LAXAPHYCINS A, B, D AND E

• Published in: Journal of antibiotics Vol. 45; no. 9; pp. 1458 - 1466
• Main Authors: FRANKMÖLLE, WALTER P., KNÜBEL, GEORG, MOORE, RICHARD E., PATTERSON, GREGORY M. L.
• Format: Journal Article
• Language: English
• Published: Japan JAPAN ANTIBIOTICS RESEARCH ASSOCIATION 1992
• Subjects: Amino Acid Sequence; Antifungal Agents - chemistry; Antifungal Agents - isolation & purification; Cyanobacteria - chemistry; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Peptides, Cyclic - chemistry; Peptides, Cyclic - isolation & purification; Structure-Activity Relationship
• ISSN: 0021-8820; 1881-1469
• DOI: 10.7164/antibiotics.45.1458

Laxaphycins A and B are the major components in an antifungal mixture of cyclic peptides from the terrestrial blue-green alga Anabaena laxa FK-1-2. NMR and MS spectral studies coupled with amino acid analysis indicate that the gross structures of laxaphycins A and B are cyclic (Aoc-Hse-E-Dhb-Hyp-Hse-Phe-Leu-Ile-Ile-Leu-Gly) where Aoc is a 3-aminooctanoic acid residue and cyclic (Ala-Hleu-Gln-N-Melle-Hasn-Thr-Pro-Leu-Thr-Ade-Val-Hleu) where Ade is a 3-aminodecanoyl unit, respectively. Laxaphycin E, a minor cyclic undecapeptide, differs in gross structure from laxaphycin A in possessing a 3-aminodecanoic acid unit (Ade) in lieu of Aoc, whereas laxaphycin D, a minor cyclic dodecapeptide, differs from laxaphycin B in possessing a 3-aminooctanoyl unit (Aoc) instead of an Ade unit.