5626
T. K. Chakraborty et al. / Tetrahedron Letters 45 (2004) 5623–5627
Bechowski, H. B.; Hriby, V. J.; Davis, T. P. Peptides 1999,
20, 1229–1238; (c) Romanowski, M.; Zhu, X.; Misicka, A.;
Lipkowski, A. W.; Hruby, V. J.; O’Brien, D. F. Biochim.
Biophys. Acta 1997, 1329, 245–258; (d) Burton, P. S.;
Condari, R. A.; Hilgers, N. F. H.; Borchardt, R. T.
J. Pharm. Sci. 1996, 85, 1336–1340.
It is worth noting here that unlike in sugars with free
hydroxyls, where an unusual pseudo b-turn with a
9-membered H-bond was observed between AAiþ2
-
NH fi AAi-C3OH (AAi is Gaa),6 in the fatty acylated
furanoid sugar amino acid-containing peptide 4, we
observed a 10-membered H-bond between AAiþ1
-
6. (a) Chakraborty, T. K.; Ghosh, S.; Jayaprakash, S.;
Sarma, J. A. R. P.; Ravikanth, V.; Diwan, P. V.; Nagaraj,
R.; Kunwar, A. C. J. Org. Chem. 2000, 65, 6441–6457; (b)
Chakraborty, T. K.; Jayaprakash, S.; Diwan, P. V.;
Nagaraj, R.; Jampani, S. R. B.; Kunwar, A. C. J. Am.
Chem. Soc. 1998, 120, 12962–12963.
NH fi AAiÀ1-CO (AAi is Gaa). This feature is similar to
those reported by us earlier in benzyl-protected Gaa
oligomers18 and by Fleet et al. in acetate- and acetonide-
protected examples.19 Further work on these fatty
acylated furanoid sugar amino acids is in progress.
7. Simple di-O-acetyl furanoid sugar amino acids have been
prepared by Fleet’s group earlier: Smith, M. D.; Long, D.
D.; Marquess, D. G.; Claridge, T. D. W.; Fleet, G. W. J.
Chem. Commun. 1998, 2039–2040.
8. Chakraborty, T. K.; Ghosh, S. J. Indian Inst. Sci. 2001, 81,
117–123.
Acknowledgements
The authors wish to thank DST, New Delhi for financial
support (T.K.C.) and CSIR, New Delhi for research
fellowships (B.K.M. and S.U.K.).
9. Corey, E. J.; Samuelsson, B. J. Org. Chem. 1984, 49, 4735.
10. Selected physical data of 1: 1H NMR (DMSO-d6,
500 MHz) d 7.02 (br t, J ¼ 6:4 Hz, 1H, NHBoc), 5.28
(m, 1H, C3-H), 4.97 (m, 1H, C4-H), 4.48 (d, J ¼ 4:8 Hz,
1H, C2-H), 3.84 (ddd, J ¼ 9:1, 6.1, 1.8 Hz, 1H, C5-H),
3.26 (m, 2H, C6-H2), 2.35–2.20 (m, 4H, –OCOCH2–),
1.58–1.20 (m, 4H, –OCOCH2CH2–), 1.38 (s, 9H, Boc),
0.86 (m, 6H, methyls); MS (ESI) m=z (%) 416 (100)
References and notes
1
[M)H]þ. Selected physical data of 2: H NMR (DMSO-
1. (a) Green, I.; Christison, R.; Voyce, C. J.; Bundell, K. R.;
Lindsay, M. A. Trends Pharmacol. Sci. 2003, 24, 213–215;
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92, 1754–1772; (c) Schwarze, S. R.; Hruska, K. A.;
Dowdy, S. F. Trends Cell Biol. 2000, 10, 290–295; (d)
Lindgren, M.; Hallbrink, M.; Prochiantz, A.; Langel, U.
Trends Pharmacol. Sci. 2000, 21, 99–103; (e) Schwarze, S.
R.; Dowdy, S. F. Trends Pharmacol. Sci. 2000, 21, 45–48;
(f) Stein, W. D. Transport and Diffusion Across Cell
Membranes; Academic: San Diego, 1986.
2. (a) Pantarotto, D.; Briand, J.-P.; Prato, M.; Bianco, A.
Chem. Commun. 2004, 16–17; (b) Malkia, A.; Liljeroth, P.;
Kontturi, K. Chem. Commun. 2003, 1430–1431; (c) Bogu-
slavsky, V.; Hruby, V. J.; O’Brien, D. F.; Misicka, A.;
Lipkowski, A. W. J. Peptide Res. 2003, 61, 287–297; (d)
Savic, R.; Luo, L.; Eisenberg, A.; Maysinger, D. Science
2003, 300, 615–618.
d6, 500 MHz) d 8.37 (br t, J ¼ 6:3 Hz, 1H, NHBoc), 4.80
(m, 1H, C3-H), 4.09 (m, 1H, C4-H), 4.05 (br d, J ¼ 4:8 Hz,
1H, C2-H), 3.76 (ddd, J ¼ 8:8, 6.3, 1.8 Hz, 1H, C5-H),
3.26 (m, 2H, C6-H2), 2.28–2.06 (m, 4H, –OCOCH2–),
1.48–1.28 (m, 20H, –CH2–), 1.24 (s, 9H, Boc), 0.84 (m, 6H,
methyls); MS (ESI) m=z (%) 452 (100) [M+Na)Boc]þ.
26
Selected physical data of 3: ½aꢀ 10.45 (c 0.0034, CHCl3);
D
IR (KBr) mmax 2925, 2854, 1745, 1515, 1219, 1164,
772 cmÀ1 1H NMR (DMSO-d6, 200 MHz) d 7.00 (t,
;
J ¼ 6:4, 1H, NHBoc), 5.3 (m, 1H, C3-H), 5.00 (m, 1H,
C4-H), 4.6 (d, J ¼ 4:8 Hz, 1H, C2-H), 3.88 (ddd, J ¼ 8:8,
6.4, and 1.9 Hz, 1H, C5-H), 3.16 (m, 2H, C6-H2), 2.30–
2.15 (m, 4H, –OCOCH2–), 1.47–1.39 (m, 4H, –OC-
OCH2CH2–), 1.4 (s, 9H, Boc), 1.19–1.39 (m, 40 H,
–CH2–), 0.83 (t, J ¼ 5:7 Hz, 6H, methyls); MS (LSIMS)
m=z (%) 721 (15) [M+H+Na]þ.
11. (a) Bodanszky, M.; Bodanszky, A. The Practices of
Peptide Synthesis; Springer: New York, 1984; (b) Grant,
G. A. Synthetic Peptides: A User’s Guide; W.H. Freeman:
New York, 1992; (c) Bodanszky, M. Peptide Chemistry: A
€
3. For some representative works see: (a) Lowik, D. W. P.
M.; Linhardt, J. G.; Adams, P. J. H. M.; van Hest, J. C.
M. Org. Biomol. Chem. 2003, 1, 1827–1829; (b) Foldvari,
M.; Baca-Estrada, M. E.; He, Z.; Hu, J.; Attah-Poku, S.;
King, M. Biotechnol. Appl. Biochem. 1999, 30, 129–137; (c)
Foldavari, M.; Attah-Poku, S.; Hu, J.; Li, Q.; Hughes, H.;
Babiuk, L. A.; Kruger, S. J. Pharm. Sci. 1998, 87, 1203–
1208; (d) Sankaram, M. B. Biophys. J. 1994, 67, 105–112;
(e) Muranishi, S.; Sakai, A.; Yamada, K.; Murakami, M.;
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Hashimoto, M.; Takada, K.; Kiso, Y.; Muranishi, S.
Pharm. Res. 1989, 6, 171–176.
Practical Textbook; Springer: Berlin, 1993.
26
12. Selected physical data of 4: ½aꢀ 14.16 (c 0.0037, CHCl3);
D
IR (KBr) mmax 3414, 2926, 1656, 1219, 771 cmÀ1; 1H NMR
(DMSO-d6, 200 MHz) listed in Table 1; MS (LSIMS) m=z
(%) 1135 (30) [M+H]þ.
13. (a) Cavanagh, J.; Fairbrother, W. J.; Palmer, A. G., III;
Skelton, N. J. Protein NMRSpectroscopy ; Academic: San
€
Diego, 1996; (b) Wuthrich, K. NMRof Proteins and
Nucleic Acids; Wiley: New York, 1986.
14. Hwang, T. L.; Shaka, A. J. J. Am. Chem. Soc. 1992, 114,
3157–3159.
4. For reviews on sugar amino acids see: (a) Gruner, S. A.
W.; Locardi, E.; Lohof, E.; Kessler, H. Chem. Rev. 2002,
102, 491–514; (b) Chakraborty, T. K.; Ghosh, S.; Jaya-
prakash, S. Curr. Med. Chem. 2002, 9, 421–435; (c)
Chakraborty, T. K.; Jayaprakash, S.; Ghosh, S. Comb.
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Schweizer, F. Angew. Chem., Int. Ed. 2002, 41, 230–253;
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Chemtracts Org. Chem. 2001, 14, 481–499.
15. (a) Adams, P. D.; Chen, Y.; Ma, K.; Zagorski, M. G.;
€
Sonnichsen, F. D.; McLaughlin, M. L.; Barkley, M. D.
J. Am. Chem. Soc. 2002, 124, 9278–9286; (b) Kessler, H.;
Bats, J. W.; Griesinger, C.; Koll, S.; Will, M.; Wagner, K.
J. Am. Chem. Soc. 1988, 110, 1033–1049; (c) Kessler, H.
Angew. Chem., Int. Ed. Engl. 1982, 21, 512–523.
€
16. Kessler, H.; Griesinger, C.; Lautz, J.; Muller, A.; van
5. For some relevant references see: (a) Kloosterman, D. A.;
Goodwin, J. T.; Burton, P. S.; Condari, R. A.; Scahill, T.
A.; Blinn, J. R. Biopolymers 2000, 53, 396–410; (b) Gentry,
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Gunsteren, F. W.; Berendsen, H. J. C. J. Am. Chem. Soc.
1988, 110, 3393–3396.
17. Molecular mechanics/dynamics calculations were carried
out using the Sybyl 6.8 program on a Silicon Graphics O2