Scyptolin A and B, cyclic depsipeptides from axenic cultures of Scytonema hofmanni PCC 7110.
Two novel cyclic depsipeptides were isolated from axenic cultures of the terrestrial cyanobacterium Scytonema hofmanni PCC 7110 and designated scyptolin A and B. Amino acid analyses in context with mass and 1H/13C NMR spectroscopies revealed a composition typical for heterologous cyanopeptolins but containing the uncommon residue 3'-chloro-N-methyl-Tyr (cmTyr) and a unique sidechain. Scyptolin A and B both consist of the N-acylated peptide But(1)-Ala(2)-Thr(3)-Thr(4)-Leu(5)-Ahp(6) (3-amino-6-hydroxy-2-oxo-1-piperidine)-Thr(7)-cmTyr(8)-Val(9), which forms a 19-membered ring by esterification of the carboxyl of Val(9) with the hydroxyl of Thr(4). In scyptolin B, the hydroxyl of the Thr(3) residue is additionally esterified with N-butyroyl-Ala. Both scyptolin A and B exhibit selective inhibition of porcine pancreatic elastase in vitro with IC(50) values of 3.1 microg/ml.
Matern
U
U
Institut für Biologie II (Mikrobiologie), Albert-Ludwigs-Universität, Schänzlestrasse 1, D-79104 Freiburg i. Br., Germany. matern@uni-freiburg.de
Oberer
L
L
Falchetto
R A
RA
Erhard
M
M
König
W A
WA
Herdman
M
M
Weckesser
J
J
D000595:Amino Acid Sequence; D000818:Animals; D000458:Cyanobacteria / Q000737:chemistry*; D047630:Depsipeptides; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D019906:Nuclear Magnetic Resonance, Biomolecular; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D010456:Peptides, Cyclic / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D011487:Protein Conformation; D013552:Swine
D047630:Depsipeptides; D004791:Enzyme Inhibitors; D010456:Peptides, Cyclic; C448645:scyptolin A; C448646:scyptolin B; D010196:Pancreatic Elastase