np5b00871_si_001.pdf (17.48 MB)
The Halicylindramides, Farnesoid X Receptor Antagonizing Depsipeptides from a Petrosia sp. Marine Sponge Collected in Korea
journal contribution
posted on 2016-01-28, 00:00 authored by Dongyup Hahn, Hiyoung Kim, Inho Yang, Jungwook Chin, Hoosang Hwang, Dong Hwan Won, Byoungchan Lee, Sang-Jip Nam, Merrick Ekins, Hyukjae Choi, Heonjoong KangThree new structurally related depsipeptides,
halicylindramides F–H (1–3), and two known halicylindramides were isolated from a Petrosia sp. marine sponge collected off the shore of Youngdeok-Gun, East
Sea, Republic of Korea. Their planar structures were elucidated by
extensive spectroscopic data analyses including 1D and 2D NMR data
as well as MS data. The absolute configurations of halicylindramides
F–H (1–3) were determined
by Marfey’s method in combination with Edman degradation. The
absolute configurations at C-4 of the dioxyindolyl alanine (Dioia)
residues of halicylindramides G (2) and H (3) were determined as 4S and 4R,
respectively, based on ECD spectroscopy. The C-2 configurations of
Dioia in 2 and 3 were speculated to both
be 2R based on the shared biogenesis of the halicylindramides.
Halicylindramides F (1), A (4), and C (5) showed human farnesoid X receptor (hFXR) antagonistic activities,
but did not bind directly to hFXR.