Synthesis and antimetastatic activity of L-iduronic acid-type 1-N- iminosugars

Journal of Medicinal Chemistry

Volumn 40, Issue 16, 1997, Pages 2626-2633

  Nishimura, Yoshio ^a   Satoh, Takahiko ^a   Adachi, Hayamitsu ^a   Kondo, Shinichi ^a   Takeuchi, Tomio ^a   Azetaka, Masayuki ^a,b   Fukuyasu, Harumi ^a,b   Iizuka, Yumiko ^a,b  

^a INSTITUTE OF MICROBIAL CHEMISTRY   (Japan)

^b MEIJI SEIKA KAISHA LTD   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINO GUANIDINO 5 HYDROXY 6 (TRIFLUOROACETAMIDO)PIPERIDINE 3 CARBOXYLIC ACID; 6 ACETAMIDO 4 AMINO 5 HYDROXYPIPERIDINE 3 CARBOXYLIC ACID; 6 ACETAMIDO 4 GUANIDINO 5 HYDROXYPIPERIDINE 3 CARBOXYLIC ACID; BETA GLUCURONIDASE; GLYCOSYLTRANSFERASE; HEPARANASE; IDURONIC ACID; PROTEOGLYCAN; SIASTATIN B; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTINEOPLASTIC ACTIVITY; ARTICLE; BACTERIUM CULTURE; BASEMENT MEMBRANE; CANCER INVASION; CARBOHYDRATE METABOLISM; CELL SURFACE; ENZYME ACTIVITY; ENZYME MECHANISM; EXTRACELLULAR MATRIX; IMMUNE RESPONSE; LUNG METASTASIS; MOUSE; NONHUMAN; STREPTOMYCES;

ANIMALS; ANTINEOPLASTIC AGENTS; ENZYME INHIBITORS; IDURONIC ACID; LUNG NEOPLASMS; MICE; MODELS, CHEMICAL; NEOPLASM METASTASIS; PIPERIDINES; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR CELLS, CULTURED;

EID: 0030849977     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm960627l     Document Type: Article

References (63)

1. Rademacher, T. W.; Parekh, K. B.; Dwek, R. A. Glycobiology. In Annual Review of Biochemistry; Richardson, C. C., Ed.; Stanford University Press: Palo Alto, CA, 1988; Vol. 57, pp 785-833.
2. Sharon, N.; Lis, H. Lectins as cell recognition molecules. Science 1989, 246, 227-234.
3. Karlsson, K.-A. Glycobiology: A growing field for drug design. Trends Pharmacol. Sci. 1991, 12, 265-272.
4. Drickamer, K.; Carver, J. Carbohydrates and glycoconjugates: Upwardly mobile sugars gain status as information-bearing molecules. Curr. Opin. Struct. Biol. 1992, 2, 653-654.
5. Sharon, N.; Lis, H. Carbohydrates in cell recognition. Sci. Am. 1993, 268, 74-81.
6. (a) Fidler, I. J.; Gersten, D. M.; Hart, I. R. The biology of cancer invasion and metastasis. Adv. Cancer Res. 1978, 28, 149-250.
7. (b) Fidler, I. J. Tumor heterogeneity and the biology of cancer invasion and metastasis. Cancer Res. 1978, 38, 2651-2660.
8. (c) Poste, G.; Fidler, I. J. The pathogenesis of cancer metastasis. Nature (London) 1980, 283, 139-146.
9. (d) Liotta, L. A. Tumor invasion and metastasis-role of the extracellular matrix: Rhoads Memorial Award Lecture. Cancer Res. 1986, 46, 1-7.
10. (e) Nicolson, G. L. Metastatic tumor cell interactions with endothelium, basement membrane and tissue. Curr. Opin. Cell. Biol. 1989, 1, 1009-1019.
11. (a) Klein, U.; von Figura, K. Partial purification and characterization of a heparan sulfate specific endoglucuronidase. Biochem. Biophys. Res. Commun. 1976 73, 569-576.
12. (b) Thuberg, L.; Baeckstroem, G.; Wasteson, A.; Robinson, H. G.; Oegren, S.; Lindahl, U. Enzymatic depolymerization of heparin-related polysaccharides. J. Biol. Chem. 1982, 257, 10278-10282.
13. (c) Oldberg, A.; Heldin, C.-H.; Wasteson, Å.; Busch, C.; Hoeoek, M. Characterization of platelet endoglycosidase degrading heparin-like polysaccharides. Biochemistry 1980, 19, 5755-5762.
14. (d) Oosta, G. M.; Favreu, L. V.; Beeler, D. L.; Rosenberg, R. D. Purification and properties of human platelet heparitinase. J. Biol. Chem. 1982, 257, 11249-11255.
15. (e) Nakajima, M.; Irimura, T.; Di Ferrante, N.; Nicolson, G. L. Metastatic melanoma cell heparanase. J. Biol. Chem. 1984, 259, 2283-2290.
16. (a) Matalon, R.; Cifonelli, J. A.; Dorfman, A. L-Iduronidase in cultured human fibroblasts and liver. Biochem. Biophys. Res. Commun. 1971, 42, 340-345.
17. (b) Bach, G.; Friedman, R.; Weissman, B.; Neufeld, E. F. Defect in the Hurler and Scheie syndromes. Deficiency of α-L-iduronidase. Proc. Natl. Acad. Sci. U.S.A. 1972, 69, 2048-2051.
18. (c) Roden, L. Structure and metabolism of connective tissue proteoglycans. In The Biochemistry of Glycoproteins and Proteoglycans; Lennarz, W. J., Ed.; Plenum Press: New York, 1980; pp 267-371.
19. (d) Takagaki, K.; Nakamura, T.; Majima, M.; Endo, M. Isolation and characterization of a chondroitin sulfate-degrading endo-β-glucuronidase from rabbit liver. J. Biol. Chem. 1988, 263, 7000-7006.
20. (a) Nakajima, M.; Irimura, T.; Nicolson, G. L. Heparanase and tumor metastasis. J. Cell. Biochem. 1988, 36, 157-167.
21. (b) Irimura, T.; Nakajima, M.; Nicolson, G. L. Chemically modified heparins as inhibitors of heparan sulfate specific-beta-glucuronidase (heparanase) of metastatic melanoma cells. Biochemistry 1986, 25, 5322-5328.
22. (c) Keren, Z.; Leland, F.; Nakajima, M.; Legrue, S. J. Inhibition of experimental metastasis and extracellular matrix degradation by butanol extracts from B16-F1 murine melanoma. Cancer Res. 1989, 49, 295-300.
23. (d) Nakajima, M.; DeChavigny, A.; Johnson, C. E.; Hamada, J.-I.; Stein, C. A.; Nicolson, G. L. Suramin. A potent inhibitor of melanoma heparanase and invasion. J. Biol. Chem. 1991, 266, 9661-9666.
24. Umezawa, H.; Aoyagi, T.; Komiyama, T.; Morishima, H.; Hamada, M.; Takeuchi, T. Purification and characterization of a sialidase inhibitor, siastatin, produced by Streptomyces. J. Antibiot. 1974, 27, 963-969.
25. (a) Nishimura, Y.; Kudo, T.; Kondo, S.; Takeuchi, T. Totally synthetic analogues of siastatin B II. Optically active piperidine derivatives having trifluoroacetamide and hydroxyacetamide groups at C-2. J. Antibiot. 1992, 45, 963-970.
26. (b) Nishimura, Y.; Kudo, T.; Kondo, S.; Takeuchi, T. Totally synthetic analogues of siastatin B III. Trifluoroacetamide analogues having inhibitory activity for tumor metastasis. J. Antibiot. 1994, 47, 101-107.
27. (c) Nishimura, Y.; Satoh, T.; Kondo, S.; Takeuchi, T. Effect on spontaneous metastasis of mouse Lewis lung carcinoma by a trifluoroacetamide analogue of siastatin B. J. Antibiot. 1994, 47, 840-842.
28. (a) Nishimura, Y. Stereoselective synthesis and transformation of siastatin B, a novel glycosidase inhibitors, directed toward new drugs for viral infection and tumor metastasis. In Studies in Natural Products Chemistry; Atta-ur-Rahman, Ed.; Elsevier: Amsterdam, 1995; Vol. 16, pp 75-121.
29. (b) Ichikawa, M.; Igarashi, Y.; Ichikawa, Y. Facile synthesis of glucose-type 1-N-iminosugars: New inhibitor of glycolipid biosynthesis. Tetrahedron Lett. 1995, 36, 1767-1770.
30. (c) Jespersen, T. M.; Dong, W.; Sierks, M. R.; Skrydstrup, T.; Lundt, I.; Bols, M. Isofagomine, a potent, new glycosidase inhibitor. Angew. Chem., Int. Ed. Engl. 1994, 33, 1778-1779.
31. Kawase, Y.; Takahashi, M.; Takatsu, T.; Arai, M.; Nakajima, M.; Tanzawa, K. A-72363 A-1, A-2 and C, novel heparanase inhibitors from Streptomyces nobilis SANK 60192 II. Biological activities. J. Antibiot. 1996, 49, 61-64.
32. Nishimura, Y.; Satoh, T.; Adachi, H.; Kondo, S.; Takeuchi, T.; Azetaka, M.; Fukuyasu, H.; Iizuka, Y. The first L-iduronic acid-type 1-N-iminosugars having inhibitory activity of experimental metastasis. J. Am. Chem. Soc. 1996, 118, 3051-3052.
33. (a) Nishimura, Y.; Kudo, T.; Umezawa, Y.; Kondo, S.; Takeuchi, T. Design of potential neuraminidase inhibitors by dehydration, deoxygenation and epimerization of siastatin B. Nat. Prod. Lett. 1992. 1, 39-44.
34. (b) Nishimura, Y.; Umezawa, Y.; Kondo, S.; Takeuchi, T.; Mori, K.; Kijima-Suda, I.; Tomita, K.; Sugawara, K.; Nakamura, K. Synthesis of 3-episiastatin B analogues having anti-influenza virus activity. J. Antibiot. 1993, 46, 1883-1889.
35. Alonso, R. A.; Burgey, C. S.; Rao, B. V.; Vite, G. D.; Vollerthun, R.; Zottola, M. A.; Fraser-Reid, B. Carbohydrates to carbocycles: Synthesis of the densely functionalized carbocyclic core of tetrodotoxin by radical cyclization of an anhydro sugar precursor. J. Am. Chem. Soc. 1993, 115, 6666-6672.
36. Kudo, T.; Nishimura, Y.; Kondo, S.; Takeuchi, T. Synthesis of the potent inhibitors of neuraminidase, N-(1,2-dihydroxypropyl)-derivatives of siastatin B and its 4-deoxy analogs. J. Antibiot. 1993, 46, 300-309.
37. Gent, P. A.; Gigg, R.; May, S.; Conant, R. Phenyloxazoline derivative of amino-sugars. Part II. The fission of phenyloxazolines under basic conditions. J. Chem. Soc., Perkin Trans. 1 1972, 2748-2750.
38. Weygand, F.; Frauendorfer, E. N-(Trifluoroacetyl)amino acids. XXI. Reductive elimination of the N-trifluoroacetyl and N-trichloroacetyl groups by sodium borohydride and applications in peptide chemistry. Chem. Ber. 1970, 103, 2437-2449.
39. Lednicer, D.; Mitscher, L. A. The Organic Chemistry of Drug Synthesis; Wiley: New York, 1977; Vol. 1, pp 1-432 and 1980; Vol. 2, pp 1-482.
40. Lednicer, D.; Mitscher, L. A. The Organic Chemistry of Drug Synthesis; Wiley: New York, 1977; Vol. 1, pp 1-432 and 1980; Vol. 2, pp 1-482.
41. (a) von Itzstein, M.; Wu, W.-Y.; Kok, G. B.; Pegg, M. S.; Dyason, J. C.; Jin, B.; Van Phan, T.; Smythe, M. L.; White, H. F.; Oliver, S. W.; Colman, P. M.; Varghese, J. N.; Ryan, D. M.; Woods, J. M.; Bethell, R. C.; Hotham, V. J.; Cameron, J. M.; Penn, C. R. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 1993, 363, 418-423.
42. (b) Woods, J. M.; Bethell, R. C.; Coates, J. A. V.; Healy, N.; Hiscox, S. A.; Peason, B. T.; Ryan, D. M.; Ticehurst, J.; Tilling, J.; Walcott, S. M.; Penn, C. R. 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro. Antimicrob. Agents Chemother. 1993, 37, 1473-1479.
43. (c) Colman, P. M. Influenza virus neuraminidase: Structure, antibodies, and inhibitors. Protein Sci. 1994, 3, 1687-1696.
44. Kim, K. S.; Qian, L. Improved method for the preparation of guanidines. Tetrahedron Lett. 1993, 34, 7677-7680.
45. Satoh, T.; Nishimura, Y.; Kondo, S.; Takeuchi, T.; Azetaka, M.; Fukuyasu, H.; Iizuka, Y.; Ohuchi, S. Synthesis and antimetastatic activity of 6-trichloroacetamido and 6-guanidino analogues of siastatin B. J. Antibiot. 1996, 49, 321-325.
46. Carlsen, P. H. J.; Katsuki, T.; Martin, V. S.; Sharpless, K. B. A greatly improved procedure for ruthenium tetraoxide catalyzed oxidations of organic compounds. J. Org. Chem. 1981, 46, 3936-3938.
47. All enzymes were purchased from Sigma Chemical Company. (a) Halvorson, H. O.; Fllias, L. C. Purification and properties of an α-glucosidase of Saccharomyces italicus Y1225. Biochim. Biophys. Acta 1958, 30, 28-40. (b) Kobayashi, A. Biochemical studies on cycasin. I. Purification and properties of cycad β-glucosidase. Agric. Biol. Chem. 1962, 26, 203-207. (c) Li, Y.-T. Studies on the glycosidases in Jack bean meal. J. Biol. Chem. 1967, 242, 5474-5480. (d) Craven, G. R.; Steers, Jr., E.; Anfinsen, C. B. Purification, composition, and molecular weight of the β-galactosidase of Escherichia coli K12. J. Biol. Chem. 1965, 240, 2468-2477. (e) Stahl, P. P. D.; Fishman, W. H. β-D-Glucuronidase. β-D-Glucuronide glucuronosohydrolase, EC 3.2.1.31. In Methods of Enzymatic Analysis; Voigt, K. D., Ed.; Academic Press: New York, 1974; Vol. 4, pp 246-256. (f) Uda, Y.; Li, S.-C.; Li, Y.-T.; McKibbin, J. M. α-N-Acetylgalactosaminidase from the limpet, Patella vulgata. J. Biol. Chem. 1977, 252, 5194-5200. (g) Tarentino, A. L.; Maley, F. β-N-Acetylglucosaminidase from Hen Oviduct. In Methods in Enzymology; Ginsburg, V., Ed.; Academic Press: New York and London, 1972; Vol. 28; pp 772-776.
48. All enzymes were purchased from Sigma Chemical Company. (a) Halvorson, H. O.; Fllias, L. C. Purification and properties of an α-glucosidase of Saccharomyces italicus Y1225. Biochim. Biophys. Acta 1958, 30, 28-40. (b) Kobayashi, A. Biochemical studies on cycasin. I. Purification and properties of cycad β-glucosidase. Agric. Biol. Chem. 1962, 26, 203-207. (c) Li, Y.-T. Studies on the glycosidases in Jack bean meal. J. Biol. Chem. 1967, 242, 5474-5480. (d) Craven, G. R.; Steers, Jr., E.; Anfinsen, C. B. Purification, composition, and molecular weight of the β-galactosidase of Escherichia coli K12. J. Biol. Chem. 1965, 240, 2468-2477. (e) Stahl, P. P. D.; Fishman, W. H. β-D-Glucuronidase. β-D-Glucuronide glucuronosohydrolase, EC 3.2.1.31. In Methods of Enzymatic Analysis; Voigt, K. D., Ed.; Academic Press: New York, 1974; Vol. 4, pp 246-256. (f) Uda, Y.; Li, S.-C.; Li, Y.-T.; McKibbin, J. M. α-N-Acetylgalactosaminidase from the limpet, Patella vulgata. J. Biol. Chem. 1977, 252, 5194-5200. (g) Tarentino, A. L.; Maley, F. β-N-Acetylglucosaminidase from Hen Oviduct. In Methods in Enzymology; Ginsburg, V., Ed.; Academic Press: New York and London, 1972; Vol. 28; pp 772-776.
49. All enzymes were purchased from Sigma Chemical Company. (a) Halvorson, H. O.; Fllias, L. C. Purification and properties of an α-glucosidase of Saccharomyces italicus Y1225. Biochim. Biophys. Acta 1958, 30, 28-40. (b) Kobayashi, A. Biochemical studies on cycasin. I. Purification and properties of cycad β-glucosidase. Agric. Biol. Chem. 1962, 26, 203-207. (c) Li, Y.-T. Studies on the glycosidases in Jack bean meal. J. Biol. Chem. 1967, 242, 5474-5480. (d) Craven, G. R.; Steers, Jr., E.; Anfinsen, C. B. Purification, composition, and molecular weight of the β-galactosidase of Escherichia coli K12. J. Biol. Chem. 1965, 240, 2468-2477. (e) Stahl, P. P. D.; Fishman, W. H. β-D-Glucuronidase. β-D-Glucuronide glucuronosohydrolase, EC 3.2.1.31. In Methods of Enzymatic Analysis; Voigt, K. D., Ed.; Academic Press: New York, 1974; Vol. 4, pp 246-256. (f) Uda, Y.; Li, S.-C.; Li, Y.-T.; McKibbin, J. M. α-N-Acetylgalactosaminidase from the limpet, Patella vulgata. J. Biol. Chem. 1977, 252, 5194-5200. (g) Tarentino, A. L.; Maley, F. β-N-Acetylglucosaminidase from Hen Oviduct. In Methods in Enzymology; Ginsburg, V., Ed.; Academic Press: New York and London, 1972; Vol. 28; pp 772-776.
50. All enzymes were purchased from Sigma Chemical Company. (a) Halvorson, H. O.; Fllias, L. C. Purification and properties of an α-glucosidase of Saccharomyces italicus Y1225. Biochim. Biophys. Acta 1958, 30, 28-40. (b) Kobayashi, A. Biochemical studies on cycasin. I. Purification and properties of cycad β-glucosidase. Agric. Biol. Chem. 1962, 26, 203-207. (c) Li, Y.-T. Studies on the glycosidases in Jack bean meal. J. Biol. Chem. 1967, 242, 5474-5480. (d) Craven, G. R.; Steers, Jr., E.; Anfinsen, C. B. Purification, composition, and molecular weight of the β-galactosidase of Escherichia coli K12. J. Biol. Chem. 1965, 240, 2468-2477. (e) Stahl, P. P. D.; Fishman, W. H. β-D-Glucuronidase. β-D-Glucuronide glucuronosohydrolase, EC 3.2.1.31. In Methods of Enzymatic Analysis; Voigt, K. D., Ed.; Academic Press: New York, 1974; Vol. 4, pp 246-256. (f) Uda, Y.; Li, S.-C.; Li, Y.-T.; McKibbin, J. M. α-N-Acetylgalactosaminidase from the limpet, Patella vulgata. J. Biol. Chem. 1977, 252, 5194-5200. (g) Tarentino, A. L.; Maley, F. β-N-Acetylglucosaminidase from Hen Oviduct. In Methods in Enzymology; Ginsburg, V., Ed.; Academic Press: New York and London, 1972; Vol. 28; pp 772-776.
51. All enzymes were purchased from Sigma Chemical Company. (a) Halvorson, H. O.; Fllias, L. C. Purification and properties of an α-glucosidase of Saccharomyces italicus Y1225. Biochim. Biophys. Acta 1958, 30, 28-40. (b) Kobayashi, A. Biochemical studies on cycasin. I. Purification and properties of cycad β-glucosidase. Agric. Biol. Chem. 1962, 26, 203-207. (c) Li, Y.-T. Studies on the glycosidases in Jack bean meal. J. Biol. Chem. 1967, 242, 5474-5480. (d) Craven, G. R.; Steers, Jr., E.; Anfinsen, C. B. Purification, composition, and molecular weight of the β-galactosidase of Escherichia coli K12. J. Biol. Chem. 1965, 240, 2468-2477. (e) Stahl, P. P. D.; Fishman, W. H. β-D-Glucuronidase. β-D-Glucuronide glucuronosohydrolase, EC 3.2.1.31. In Methods of Enzymatic Analysis; Voigt, K. D., Ed.; Academic Press: New York, 1974; Vol. 4, pp 246-256. (f) Uda, Y.; Li, S.-C.; Li, Y.-T.; McKibbin, J. M. α-N-Acetylgalactosaminidase from the limpet, Patella vulgata. J. Biol. Chem. 1977, 252, 5194-5200. (g) Tarentino, A. L.; Maley, F. β-N-Acetylglucosaminidase from Hen Oviduct. In Methods in Enzymology; Ginsburg, V., Ed.; Academic Press: New York and London, 1972; Vol. 28; pp 772-776.
52. All enzymes were purchased from Sigma Chemical Company. (a) Halvorson, H. O.; Fllias, L. C. Purification and properties of an α-glucosidase of Saccharomyces italicus Y1225. Biochim. Biophys. Acta 1958, 30, 28-40. (b) Kobayashi, A. Biochemical studies on cycasin. I. Purification and properties of cycad β-glucosidase. Agric. Biol. Chem. 1962, 26, 203-207. (c) Li, Y.-T. Studies on the glycosidases in Jack bean meal. J. Biol. Chem. 1967, 242, 5474-5480. (d) Craven, G. R.; Steers, Jr., E.; Anfinsen, C. B. Purification, composition, and molecular weight of the β-galactosidase of Escherichia coli K12. J. Biol. Chem. 1965, 240, 2468-2477. (e) Stahl, P. P. D.; Fishman, W. H. β-D-Glucuronidase. β-D-Glucuronide glucuronosohydrolase, EC 3.2.1.31. In Methods of Enzymatic Analysis; Voigt, K. D., Ed.; Academic Press: New York, 1974; Vol. 4, pp 246-256. (f) Uda, Y.; Li, S.-C.; Li, Y.-T.; McKibbin, J. M. α-N-Acetylgalactosaminidase from the limpet, Patella vulgata. J. Biol. Chem. 1977, 252, 5194-5200. (g) Tarentino, A. L.; Maley, F. β-N-Acetylglucosaminidase from Hen Oviduct. In Methods in Enzymology; Ginsburg, V., Ed.; Academic Press: New York and London, 1972; Vol. 28; pp 772-776.
53. All enzymes were purchased from Sigma Chemical Company. (a) Halvorson, H. O.; Fllias, L. C. Purification and properties of an α-glucosidase of Saccharomyces italicus Y1225. Biochim. Biophys. Acta 1958, 30, 28-40. (b) Kobayashi, A. Biochemical studies on cycasin. I. Purification and properties of cycad β-glucosidase. Agric. Biol. Chem. 1962, 26, 203-207. (c) Li, Y.-T. Studies on the glycosidases in Jack bean meal. J. Biol. Chem. 1967, 242, 5474-5480. (d) Craven, G. R.; Steers, Jr., E.; Anfinsen, C. B. Purification, composition, and molecular weight of the β-galactosidase of Escherichia coli K12. J. Biol. Chem. 1965, 240, 2468-2477. (e) Stahl, P. P. D.; Fishman, W. H. β-D-Glucuronidase. β-D-Glucuronide glucuronosohydrolase, EC 3.2.1.31. In Methods of Enzymatic Analysis; Voigt, K. D., Ed.; Academic Press: New York, 1974; Vol. 4, pp 246-256. (f) Uda, Y.; Li, S.-C.; Li, Y.-T.; McKibbin, J. M. α-N-Acetylgalactosaminidase from the limpet, Patella vulgata. J. Biol. Chem. 1977, 252, 5194-5200. (g) Tarentino, A. L.; Maley, F. β-N-Acetylglucosaminidase from Hen Oviduct. In Methods in Enzymology; Ginsburg, V., Ed.; Academic Press: New York and London, 1972; Vol. 28; pp 772-776.
54. Nishimura, Y.; Satoh, T.; Kudo, T.; Kondo, S.; Takeuchi, T. Synthesis and activity of 1-N-iminosugar inhibitors, siastatin B analogues for α-N-acetylgalactosaminidase and β-N-acetylglucosaminidase. BioMed. Chem. 1996, 4, 91-96.
55. 2 torsional terms. J. Am. Chem. Soc. 1977, 99, 8127-8134.
56. Stewart, J. P. P. Optimization of parameters for semiempirical methods. J. Comput. Chem. 1989, 10, 209-220.
57. (a) Woynarowska, B.; Skrincosky, D. M.; Haag, A.; Sharma, M.; Matta, K.; Bernacki, R. J. Inhibition of lectin-mediated ovarian tumor cell adhesion by sugar analogs. J. Biol. Chem. 1994, 269, 22797-22803.
58. (b) Woynarowska, B.; Dimitroff, C. J.; Sharma, M.; Matta, K.; Bernacki, R. J. Inhibition of human HT-29 colon carcinoma cell adhesion by a 4-fluoro-glucosamine analog. Glycoconjugate J. 1996, 13, 663-674.
59. Albini, A.; Iwamoto, Y.; Kleinman, H. R.; Aaronson, S. A.; Kozlowski, J. M.; McEwan, R. N. A rapid in vivo assay for quantitating the invasive potential of tumor cells. Cancer Res. 1987, 47, 3239-3245.
60. Saiki, I.; Murata, J.; Watanabe, K.; Fujii, H.; Abe, F.; Azuma, I. Inhibition of tumor cell invasion by ubenimex (bestatin) in vitro. Jpn. J. Cancer Res. 1989, 80, 873-878.
61. Humphries, M. J.; Matsumoto, K.; White, S. L.; Olden, K. Oligosaccharide modification by swainsonine treatment inhibits pulmonary colonization by B16-F10 murine melanoma cells. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 1752-1756.
62. Fidler, I. J. General consideration for studies of experimental cancer metastasis. Methods Cancer Res. 1978, 15, 399-439.
63. Force field calculation MM2 and semi-empirical calculation PM3 incorporated in the MOPAC (ver. 6.0) package were performed on CAChe work system in one high performance desk top workstation (Power Macintosh 8100/80).