3152
M. Hamada et al. / Bioorg. Med. Chem. Lett. 13 (2003) 3151–3153
Table 1. Inhibitory activities of a-mangostin 1 and its derivatives
against sphingomyelinase (SMase)
Synthesis of 11 and 12
Exposure of bromide 86 to s-BuLi gave the corresponding
lithio derivative, which on coupling with 7 provided 9
(Scheme 2). Oxidation of the benzyl alcohol by IBX9 and
transacetalization afforded benzofenone 10, which was
hydrogenolized to give 11. Treatment of 10 with silica gel9
effected the desired cyclization to give xanthone 12.
Compd
IC50 (mg/mL)
ASMase
NSMase
11
12
16
17
5.3
5.25
24.0
34.5
10.2
8.9
72.5
>100
Synthesis of 16 and 17
2
16.5
5.15
48.5
46.5
Compound 5 was lithiated and coupled with 136 to give
the corresponding benzyl alcohol 14, which on oxidation
with IBX9 and hydrogenolysis gave benzophenone 15
(Scheme 3). While deprotection under acidic conditions
provided 16, treatment of 15 with the PPh3–CCl4 pro-
tocol,7,10 afforded xanthone 17 in moderate yield.
a-Mangostin 1
Biological Activity
Procedure
A mixture of NBD-sphingomyelin, sphingomyelinase
and a sample was incubated at 37 ꢀC for 30 min. Enzy-
matic activity in the mixture was determined by mea-
suring the fluorescence intensity of ceramide produced.
Compounds 11 and 12, carrying no prenyl group at the
right residue, maintained comparable activity to that of
1, although selectivity between ASMase and NSMase
was diminished by increase of their activities against
NSMase (Table 1). This property was similar to the case
of saturation of the olefinic bonds of the prenyl groups.2
When compared with 1 and 2, the right prenyl group
might be responsible for the selectivity against ASMase
and NSMase. In contrast, benzophenone 16 and xan-
thone 17 without the left-prenyl group, kept the selec-
tivity, while the ASMase activities reduced to ca. 1/10 of
that of 1. These observations indicated each prenyl
group might be required to express the highly selective
inhibitory activity against ASMase.
Scheme 1. (a) BnBr, K2CO3/DMF, 96%; (b) mCPBA/CH2Cl2, then
6 M HCl/MeOH, 95%; (c) Br2/CHCl3, 84%; (d) MeI, K2CO3/DMF,
97%; (e) POCl3/DMF, then MOMCl, NaH/DMF, 54%.
Acknowledgements
This work was supported by Grant-in-Aid for the 21st
Century COE program ‘KEIO Life Conjugate Chem-
istry’ from the Ministry of Education, Culture, Sports,
Science, and Technology, Japan, as well as Keio Gijyuku
Fund for the Advancement of Education and Research.
Scheme 2. (a) s-BuLi/THF, then 7, 49%; (b) IBX/PhMe–DMSO (1:1),
82%; (c) CSA/MeOH, 81%; (d) 10% Pd/C, cyclohexene/EtOH, 97%;
(e) silica gel, 74%.
References and Notes
1. Isolation: Schmid, W. Liebigs Ann. Chem. 1855, 93, 83.
Dragendorff, O. Liebigs Ann. Chem. 1930, 482, 280. Structural
determination: Yates, P.; Stout, G. H. J. Am. Chem. Soc.
1958, 80, 1691. Scheinmann, F. Chem. Commun. 1967, 1015.
Stout, G. H.; Krahn, M. M.; Yates, P.; Bhat, H. B. Chem.
Commun. 1968, 211.
2. Okudaira, C.; Ikeda, Y.; komdo, S.; Furuya, S.; Hirabaya-
shi, Y.; Koyano, T.; Saito, Y.; Umezawa, K. J. Enzym. Inhib.
2000, 15, 129.
3. (a) Chairungsrilerd, N.; Furukawa, K.; Ohta, T.; Nozoe, S.;
Ohizumi, Y. Eur. J. Pharmacol. 1996, 314, 351. (b) Tosa, H.;
Iinuma, M.; Tanaka, T.; Nozaki, H.; Ikeda, S.; Tsutsui, K.;
Scheme 3. (a) s-BuLi/THF, then 13, 41%; (b) IBX/PhMe–DMSO
(1:1), 100%; (c) 10% Pd/C, HCO2NH4/acetone, 88%; (d) TsOH/
MeOH, 94%; (e) Ph3P, CCl4/THF, then silica gel, 61%.