A. K. Misra et al. / Bioorg. Med. Chem. Lett. 11 (2001) 2667–2669
2669
3. Kannagi, R.; Hakomori, S.-I.; Imura, H. In Altered Glyco-
sylation in Tumor Cells; Reading C. L., Hakomori, S.-I.,
Marcus, D. M., Eds.; A. R. Liss: New York, 1988; p 279.
4. Fukuda, M. In Molecular Glycobiology; Fukuda, M.,
Hindsgaul, O., Eds.; IRL: Oxford, 1994; p 1.
methanol. The methanolic fraction was concentrated and fur-
ther purified on Sephadex LH-20 to give 3.
13. Partial NMR (500 MHz; D2O): H NMR: The following
common signals for the octyl aglycon were observed in D2O
1
soln:
d
1.60–1.40 (2H, OCH2CH2), 1.40–1.10 (10H,
5. Ujita, M.; McAuliffe, J.; Schwientek, T.; Almeida, R.;
Hindsgaul, O.; Clausen, H.; Fukuda, M. J. Biol. Chem. 1998,
273, 34843.
6. (a) McAuliffe, J. C.; Fukuda, M.; Hindsgaul, O. Bioorg.
Med. Chem. Lett. 1999, 9, 2855 and the references cited
therein. (b) Koeller, K. M.; Wong, C.-H. Chem. Eur. J. 2000,
6, 1243. (c) Reddy, G. V.; Jain, R. K.; Locke, R. D.; Matta,
K. L. Carbohydr. Res. 1996, 280, 261.
OCH2CH2(CH2)5CH3), 0.85 (t, 3H, octyl CH3). H-1 indicates
the anomeric proton of the GalNAc residue, H-10 the anome-
ric proton of the Gal residue linked to O-3 of the GalNAc and
H-100 the anomeric proton of the GlcNAc residue linked to O-
6 of the GalNAc and onwards. 1: d 4.83 (d, J1,2=3.6 Hz, 1H,
H-1), 4.52 (d, J1 ,2 =7.8Hz, 1H, H-1 00), 4.42 (2d, J1 ,2 =7.8
00 00
0
0
=7.8Hz, 2H, H-1 0 and H-1000), 4.26 (dd, 1H, H-
000, 2000
Hz and J1
3), 4.17 (bs, 1H, H-4), 2.0 and 2.02 (2s, each 3H, 2 NHAc); 13
C
7. Lonn, H. Carbohydr. Res. 1985, 139, 105.
NMR: d 105.4, 103.7, 102.2 and 97.5. 2: d 4.86 (0d0 , J1,2=3.5
00 00
8. Yule, J. E.; Wong, T. C.; Gandhi, S. S.; Qiu, D.; Riopel,
M. A.; Koganty, R. R. Tetrahedron Lett. 1995, 36, 6839.
9. Fugedi, P.; Garegg, P. J. Carbohydr. Res. 1986, 149, C9.
10. General procedure for glycosylation: a mixture of 11, 8, or
5 (1.2 mmol), acceptor sugars 10, 13, or 15 (1.0 mmol), MS-4
Hz, 1H, H-1), 4.71 (d, J1 ,2 =7.5 Hz, 1H, H-1 ), 4.53 (d,
0000 0000
J1
=8.0 Hz, 1H, H-10000), 4.47 (3d, J=7.5 Hz each, 3H, H-
,2
10, H-1000 and H-100000), 4.30 (dd, 1H, H-3), 4.19 (bs, 1H, H-4),
4.13 (bs, 1h, H-4000), 1.99, 2.0 and 2.02 (3s, each 3H, 3 NHAc;
13C NMR: d 105.3, 103.5, 103.5, 103.4, 102.1 and 97.3. 3: d
0
0
A (4 g) and DMTST (4.8mmol) in CH Cl2 (20 mL) was stir-
2
4.86 (d, J1,2=3.0 Hz, 1H, H-1), 4.52 (d, J1 ,2 =8.5 Hz, 1H, H-
red at ꢁ10 or 0 ꢀC for 8to 12 h. Dilution with CH Cl2 was
10), 4.46 (d, J1 ,2 =8.0 Hz, 1H, H-1 ), 4.30 (dd, 1H, H-3), 4.21
00
00 00
2
followed by filtration through Celite. The organic layer was
washed with satd NaHCO3, water, dried (Na2SO4) and con-
centrated. Column chromatography on SiO2 using toluene–
EtOAc as solvent gave the pure glycosylation products.
11. Van Boeckel, C. A. A.; Beetz, T. Tetrahedron Lett. 1983,
24, 3775.
(bs, 1H, H-4), 2.02 and 2.01 (2s, each 3H, 2 NHAc); 13C
NMR: d 105.3, 102.1, 97.2. 4: d 4.86 (d, J1,2=3.5 Hz, 1H, H-
00
00 00
0000,20000
1), 4.70 (d, J1 ,2 =9.0 Hz, 1H, H-1 ), 4.54 (d, J1
=8.0 Hz,
1H, H-10000), 4.47 (2d, J=7.5 Hz each, 2H, H-10 and H-1000),
4.30 (dd, 1H, H-3), 4.20 (bs, 1H, H-4), 4.14 (bs, 1H, H-4000),
1.99, 2.0 and 2.02 (3s, each 3H, 3 NHAc); 13C NMR: d 105.2,
103.4 (2ꢂC), 102.0, 97.2.
12. Typical procedure for enzymatic digestion: to a solution
of compound 1 (1 mg, 1.16 mmol) in 190 mL of 50 mM sodium
citrate buffer was added b-galactosidase (EC 3.2.1.23; jack
bean; 1 U, 10 mL) and the solution was kept at 37ꢀC for 24 h.
The reaction mixture was applied to a C18-SepPak cartridge
which was washed with water. Product was eluted with
14. HRMS: 1: calcd for C36H64O21N2 (M+Na+) 883.3894;
found 883.3910. 2: calcd for C50H87O31N3 (M+Na+)
1248.5216; found 1248.5165. 3: calcd for C30H54O16N2
(M+Na+) 721.3366; found 721.3365. 4: calcd for
C44H77O26N3 (M+Na+) 1086.4687; found 1086.4701.