TY - JOUR
T1 - The Halicylindramides, Farnesoid X Receptor Antagonizing Depsipeptides from a Petrosia sp. Marine Sponge Collected in Korea
AU - Hahn, Dongyup
AU - Kim, Hiyoung
AU - Yang, Inho
AU - Chin, Jungwook
AU - Hwang, Hoosang
AU - Won, Dong Hwan
AU - Lee, Byoungchan
AU - Nam, Sang Jip
AU - Ekins, Merrick
AU - Choi, Hyukjae
AU - Kang, Heonjoong
N1 - Publisher Copyright:
© 2016 The American Chemical Society and American Society of Pharmacognosy.
PY - 2016/3/25
Y1 - 2016/3/25
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84962427485&partnerID=8YFLogxK
U2 - 10.1021/acs.jnatprod.5b00871
DO - 10.1021/acs.jnatprod.5b00871
M3 - Article
C2 - 26821210
AN - SCOPUS:84962427485
SN - 0163-3864
VL - 79
SP - 499
EP - 506
JO - Journal of Natural Products
JF - Journal of Natural Products
IS - 3
ER -
