The Halicylindramides, Farnesoid X Receptor Antagonizing Depsipeptides from a Petrosia sp. Marine Sponge Collected in Korea

J Nat Prod. 2016 Mar 25;79(3):499-506. doi: 10.1021/acs.jnatprod.5b00871.

Dongyup Hahn ¹, Hiyoung Kim ², Inho Yang ², Jungwook Chin ¹, Hoosang Hwang ², Dong Hwan Won ², Byoungchan Lee ², Sang-Jip Nam ³, Merrick Ekins ⁴, Hyukjae Choi ⁵, Heonjoong Kang ²

Affiliations

1 New Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation , Daegu, 41061, Republic of Korea.
2 School of Earth and Environmental Sciences, Seoul National University , NS-80, Seoul, 08826, Republic of Korea.
3 Department of Chemistry and Nano Science, Global Top 5 Program, Ewha Womans University , Seoul, 03760, Republic of Korea.
4 Queensland Museum , P.O. Box 3300, South Brisbane, Queensland 4101, Australia.
5 College of Pharmacy, Yeungnam University , Gyeongsan, 38541, Republic of Korea.

PMID: 26821210 DOI: 10.1021/acs.jnatprod.5b00871

Abstract

Three 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.

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