Chemical structure of cichorinotoxin, a cyclic lipodepsipeptide that is produced by Pseudomonas cichorii and causes varnish spots on lettuce

• Hidekazu Komatsu,
• Takashi Shirakawa,
• Takeo Uchiyama and
• Tsutomu Hoshino

Beilstein J. Org. Chem. 2019, 15, 299–309, doi:10.3762/bjoc.15.27

• -Val14-Ala15-Val16-(Z)-dhThr17-D-alloThr18-Ala19-L-Dab20-Ser21-Val22, and an ester linkage is present between D-alloThr18 and Val22 (dhThr: 2-aminobut-2-enoic acid; Dab: 2,4-diaminobutanoic acid). Thus, the toxin is a lipodepsipeptide with 22 amino acids. The mono- and tetraacetate derivatives and two

• alkaline hydrolysates, compounds A and B, were prepared. We discuss here the structure–activity relationships between the derivatives and their necrotic activities toward lettuce. Keywords: cichorinotoxin; lipodepsipeptide; necrotic lesion of lettuce; phytotoxin; Pseudomonas cichorii; Introduction

• toxin was confirmed to have an elicitor-like effect on the production of the phytoalexin lettucenin A [6][7][8]. As described below, the toxin was determined to be a cyclic lipodepsipeptide composed of a 3-hydroxydecanoic acid moiety and 22 amino acid residues. Two types of cyclic lipodepsipeptide

A macrolactonization approach to the total synthesis of the antimicrobial cyclic depsipeptide LI-F04a and diastereoisomeric analogues

• James R. Cochrane,
• Dong Hee Yoon,
• Christopher S. P. McErlean and
• Katrina A. Jolliffe

Beilstein J. Org. Chem. 2012, 8, 1344–1351, doi:10.3762/bjoc.8.154

• group. Inversion of the D-Ala residue in the cyclic depsipeptide core resulted in complete loss of antifungal activity, indicating that the cyclic peptide conformation may be important in the biological activity of this class of cyclic lipodepsipeptide. Analytical HPLC traces of linear peptides. (a