Corpeptins, new bioactive lipodepsipeptides from cultures of Pseudomonas corrugata.
The structure of the corpeptins, bioactive lipodepsipeptides produced in culture by Pseudomonas corrugata, the causal agent of tomato pith necrosis, has been determined. The combined use of FAB-mass spectrometry, NMR spectroscopy and chemical procedures has allowed us to assign the following primary structure to the peptide moiety: Dhb-Pro-Ala-Ala-Ala-Val-Val-Dhb-Hse-Val-alle-Dhp-Ala-Ala-Ala-Val-D hb-aThr-Ala-Dab-Ser-Ile with the terminal carboxy group closing a macrocyclic ring on the hydroxy group of the allo-threonine residue. The N-terminus is in turn acylated by 3-hydroxydecanoate in corpeptin A and by cis-3-hydroxy-5-dodecenoate in corpeptin B. Some preliminary data on the biological activity of corpeptins are included.
Emanuele
M C
MC
Istituto di Strutturistica Chimica G. Giacomello, CNR, Montelibretti, Rome, Italy.
Scaloni
A
A
Lavermicocca
P
P
Jacobellis
N S
NS
Camoni
L
L
Di Giorgio
D
D
Pucci
P
P
Paci
M
M
Segre
A
A
Ballio
A
A
D000215:Acylation; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D003470:Culture Media; D003652:Decanoic Acids / Q000032:analysis; D006868:Hydrolysis; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D011549:Pseudomonas / Q000502:physiology*; D016339:Spectrometry, Mass, Fast Atom Bombardment
D003470:Culture Media; D003652:Decanoic Acids; D010456:Peptides, Cyclic; C114641:corpeptin A; C114642:corpeptin B; C017552:myrmicacin