In:
ChemBioChem, Wiley, Vol. 15, No. 7 ( 2014-05-05), p. 1021-1029
Kurzfassung:
A new cyclic hexapeptide, baceridin ( 1 ), was isolated from the culture medium of a plant‐associated Bacillus strain. The structure of 1 was elucidated by HR‐HPLC‐MS and 1D and 2D NMR experiments and confirmed by ESI MS/MS sequence analysis of the corresponding linear hexapeptide 2 . The absolute configurations of the amino acid residues were determined after derivatization by GC‐MS and Marfey's method. The cyclopeptide 1 consists partially of nonribosomal‐derived D ‐ and allo‐ D ‐configured amino acids. The order of the D ‐ and L ‐leucine residues within the sequence cyclo(‐ L ‐Trp‐ D ‐Ala‐ D ‐allo‐Ile‐ L ‐Val‐ D ‐Leu‐ L ‐Leu‐) was assigned by total synthesis of the two possible stereoisomers. Baceridin ( 1 ) was tested for antimicrobial and cytotoxic activity and displayed moderate cytotoxicity (1–2 μg mL −1 ) as well as weak activity against Staphylococcus aureus . However, it was identified to be a proteasome inhibitor that inhibits cell cycle progression and induces apoptosis in tumor cells by a p53‐independent pathway.
Materialart:
Online-Ressource
ISSN:
1439-4227
,
1439-7633
DOI:
10.1002/cbic.201300778
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
2014
ZDB Id:
2020469-3
SSG:
12
