Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2008-05-20
2008-05-20
Kam, Chih-Min (Department: 1656)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C514S002600, C514S019300, C530S300000, C530S331000, C530S333000, C530S334000, C530S345000, C424S009100
Reexamination Certificate
active
09926391
ABSTRACT:
In the present specification is disclosed a melanocyte-stimulating hormone inhibitory composition which comprises, as the active ingredient, a di- or tripeptide derivative having a certain naphthyl group or the salts thereof, or a melanocyte-stimulating hormone inhibitory compound having a 50% inhibitory concentration of cAMP production (IC50) of 100 nM or less, which composition can prevent pigmentation, or can prevent, improve or recover from immune abnormality or immunodeficiency, or regulate body weight by appetite control, and also can be used as cosmetics or external preparations for the skin, and in addition, can be produced easily, and are excellent in the stability during storage.
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S. Gerisch, et al., “Enzymatic Peptide Synthesis in Frozen Aqueous Systems: Use of Nalpha-Unprotected Unusual Acyl Donors”, Tetrahedron: Asymmetry, vol. 6, No. 12, 1995, XP-004047955, first page only.
M. Akazome, et al., “Enantiomeric Inclusion of Alpha-Hydroxy Esters by (R)-(1-Naphtyl)Glycyl-(R)-Phenylglycine and the Crystal Structures of the Inclusion Cavities”, J. Org. Chem., 64, 1999, XP-002362520, first page only.
Y. Inai, et al., “Distance and Orientation Dependence of Electron Transfer and Exciplex Formation of Naphthyl and P-Dimethylanilino Groups Fixed on a Helical Polylpeptide Chain”, J. Phys. Chem., 94, 1990, XP-002362521, first page only.
A. Janecka, et al., “Reduced-Size Antagonists of Luteinizing Hormone-Releasing Hormone Active in Vitro”, J. Med. Chem., 38, 1995, XP-002125914, pp. 2922-2924.
F.A. Etzkorn, et al., “Cyclic Hexapeptides and Chimeric Peptides as Mimics of Tendamistat”, J. Am. Chem. Soc., 116, 1994, XP-002362517, pp. 10412-10425.
C.R. Noe, et al., “Studies on Cyclic Dipeptides, I: Aryl Modifications of Cyclo-(PHE-HIS)#”, Monatshefte Fuer Chemi, 127, 1996, XP-009059933, pp. 1081-1097.
M.D. Erion, et al., “Inhibition of Peptidylglycine Alpha-Amidating Monooxygenase by N-Substituted Homocysteine Analogs”, J. Med. Chem., 37, 1994, XP-002362519, pp. 4430-4437.
H. Harada, et al., “Synthesis of Human Renin Inhibitory Peptides, Angiotensinogen Transition-State Analogs Containing a Retro-Inverso Amide Bond”, Chem. Pharm. Bull., 38 (11), 1990, XP-000919337, pp. 3042-3047.
J.R. Luly, et al., “New Inhibitors of Human Renin That Contain Novel Leu-Val Replacements”, Journal of Medicinal Chemistry, American Chemical Society. Washington, US, vol. 30, No. 8, 1987, XP-001053395, pp. 1609-1616.
S. Gerisch, et al., “Enzymatic Peptide Synthesis in Frozen Aqueous Systems: Use of Nalpha-Unprotected Unusual Acyl Donors”, Tetrahedron: Asymmetry, vol. 6, No. 12, 1995, XP-004047955, pp. 3039-3045.
M. Akazome, et al., “Enantiomeric Inclusion of Alpha-Hydroxy Esters by (R)-(1-Naphtyl)Glycyl-(R)-Phenylglycine and the Crystal Structures of the Inclusion Cavities”, J. Org. Chem., 64, 1999, XP-002362520, pp. 2293-2300.
Y. Inai, et al., “Distance and Orientation Dependence of Electron Transfer and Exciplex Formation of Naphthyl and P-Dimethylanilino Groups Fixed on a Helical Polylpeptide Chain”, J. Phys. Chem., 94, 1990, XP-002362521, pp. 6237-6243.
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A. Janecka, et al., “Reduced-Size Antagonists of Luteinizing Hormone-Releasing Hormone Active in Vitro”, J. Med. Chem., 38, 1995, XP-002125914, first page only, p. 2922-2924.
F.A. Etzkoru, et al., “Cyclic Hexapeptides and Chimeric Peptides as Mimics of Tendamistat”, J. Am. Chem. Soc., 116, 1994, XP-002362517, first page only, p. 10412-10423.
C.R. Noe, et al., “Studies on Cyclic Dipeptides, I: Aryl Modifications of Cyclo-(PHE-HIS)#”, Monatshefte Fuer Chemi, 127, 1996, XP-009059933, first page only p. 1081-1097.
M.D. Erion, et al., “Inhibition of Peptidylglycine Alpha-Amidating Monooxygenase by N-Substituted Homocysteine Analogs”, J. Med. Chem., 37, 1994, XP-002362519, first page only, p. 4430-4437.
H. Harada, et al., “Synthesis of Human Renin Inhibitory Peptides, Angiotensiogen Transition-State analogs Containing a Retro-Inverso Amide Bond”, Chem. Pharm. Bull., 38 (11), 1990, XP-000919337, first page only, p. 3042-3047.
J.R. Luly, et al., “New Inhibitors of Human Renin That Contain Novel Leu-Val Replacements”, Journal of Medicinal Chemistry, American Chemical Society. Washington, US, vol. 30, No. 9, 1987, XP-001053395, first page only, p. 1609-1616.
S. Gerisch, et al., “Enzymatic Peptide Synthesis in Frozen Aqueous Systems: Use of Nalpha-Unprotected Unusual Acyl Donors”, Tetrehedron: Asymmetry, vol. 6, No. 12, 1995, XP-004047955, first page only, p. 3039-3045.
M. Akazome, et al., “Enantiomeric Inclusion of Alpha-Hydroxy Esters by (R)-(1-Naphtyl)Glycyl-(R)-Phenylglycine and the Crystal Structures of the Inclusion Cavities”, J. Org. Chem., 64, 1999, XP-002362520, first page only, p. 2293-2300.
Y. Inai, et al., “Distance and Orientation Dependence of electron Transfer and Exciplex Formation of Naphthyl and P-Dimethylanilino Groups Fixed on a Helical Polylpeptide Chain”, J. Phys. Chem., 94, 1990, XP-002362521, first page only, p. 6237-6243.
Chujou Hiromi
Eto Yuzuru
Ijichi Chiori
Iwasaki Keiji
Sakamoto Kazutami
Ajinomoto Co. Inc.
Kam Chih-Min
Oblon & Spivak, McClelland, Maier & Neustadt P.C.
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