Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2000-09-11
2003-05-20
Huff, Sheela (Department: 1642)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C514S013800, C514S014800, C514S015800, C514S016700, C514S017400, C514S018700, C514S019300, C514S020800, C548S327500, C436S086000, C530S324000, C530S325000, C530S326000, C530S327000, C530S328000, C530S329000, C530S330000, C530S331000
Reexamination Certificate
active
06566330
ABSTRACT:
BACKGROUND OF THE INVENTION
1. Field of the Invention
This invention relates to positively charged non-natural amino acids, methods of making them and their utilization in peptides.
2. Background
Synthetic studies have been directed toward understanding the influence that only some non-natural amino acids have on the structural and biological activity of peptides.
U.S. Pat. No. 3,178,472 to Hellerbach et al. discloses a method for the conversion of amino carboxylic acids to their N-monomethyl derivatives. Naturally occurring amino acids such as alanine, phenylalanine, serine, cysteine, cystine, tyrosine, tryptophan, histidine, methionine, valine, norvaline, leucine, isoleucine, arginine, ornithine, lysine, aspartic acid, glutaminic acid, threonine, &agr;,&ggr;-diaminobutyric acid and the like are suitable starting materials. When the starting material aminocarboxylic acid contains two amino groups such as lysine, ornithine or &agr;,&ggr;-diaminiobutyric acid, then it is possible to generate a product in which one or both amino groups are methylated.
Moore et al. (
Can. J. Biochem.
1978, 56, 315) discloses the effect of the basic amino acid side chain length and the penultimate residue on the hydrolysis of benzoyldipeptides by carboxylicpeptidase B
1
(CPB). Non-natural amino acids including homolysine and homoarginine were incorporated into small peptide chains, and the kinetic parameters were determined for the CPB catalyzed hydrolysis of the peptide.
Lindeberg et al. (
Int. J. Peptide Protein Res.
1977, 10, 240) discloses the synthesis of 1-deamino-4-L-valine-8-DL-homolysine-vasopressin and protected 1-deamino-4-L-valine-8-D-lysine-vassopressin in which with non-natural amino acids were incorporated. The addition of a methylene group to lysine and arginine to generate the non-natural amino acids homolysine and homoarginine, respectively. The study revealed that peptides with homolysine and homoarginine reduced the antidiuretic activity of the peptides.
Hilpert et al. (
J. Med. Chem.
1994, 37, 3889) discloses screening of small basic molecules for binding in the recognition pocket of thrombin led to the discovery of the arginine mimetic (aminoiminomethyl)piperidine as a weak thrombin inhibitor. A number of derivatives of the arginine mimetic were prepared, and their ability to inhibit thrombin was assayed. The X-ray crystal structure analysis of thrombin as well as modeling studies of the arginine mimetic were conducted in order to rationalize the observed affinity between the unnatural amino acid and thrombin.
Nestor et al. (
J. Med. Chem.
1988, 31, 65) discloses the synthesis of a new series of unnatural amino acids and their incorporation into antagonistic analogues of lutenizing hormone-releasing hormone (LH-RH). In particular, non-natural amino acids of arginine exhibited high acute potency and very prolonged duration of action. Biological and clinical pharmacology studies revealed that these LH-RH antagonists cause mast cell degranulation, and were removed from consideration as candidates for full commercial development.
There is a need in the art for non-natural amino acids and for peptides incorporating such acids to achieve superior effects, such as, for example, improved diagnostic or disease fighting activity. None of the above references discloses the non-natural amino acids of the present invention or the advantageous properties thereof. The present invention accordingly describes positively charged non-natural amino acids, methods of making them and their utilization in peptides.
Additional advantages of the invention will be set forth in the description which follows, and in part will be obvious from the description, or may be learned by practice of the invention. The advantages of the invention will be realized and attained by means of the elements and combinations particularly pointed out in the appended claims. It is to be understood that both the foregoing general description and the following detailed description are exemplary and explanatory only and are not restrictive of the invention, as claimed.
REFERENCES:
patent: 3178472 (1965-04-01), Hellerbach et al.
patent: 3303213 (1967-02-01), Kalopissis et al.
patent: 4061542 (1977-12-01), Demny et al.
patent: 4801577 (1989-01-01), Nestor, Jr. et al.
patent: 5407916 (1995-04-01), Wise et al.
patent: 5494898 (1996-02-01), Cheng et al.
patent: 5863931 (1999-01-01), Beams et al.
patent: 6127420 (2000-10-01), Griffith et al.
patent: 3327873 (1984-02-01), None
patent: 19933701 (2001-01-01), None
patent: 0145258 (1985-06-01), None
patent: 0326766 (1989-08-01), None
patent: 0472220 (1992-02-01), None
patent: 0498941 (1992-08-01), None
patent: WO 89/01944 (1989-03-01), None
patent: WO 93/13055 (1993-07-01), None
patent: WO 94/25477 (1994-11-01), None
patent: WO 94/28921 (1994-12-01), None
patent: WO 98/17626 (1998-04-01), None
patent: WO 98/48826 (1998-11-01), None
Harper's Review of Biochemistry pp. 18-19 (1985).*
Richelson et al., “Novel Potent Neurotensin (8-13) mimetics.” Abstracts of Papers of the ACS 215: 148-Medi, Part 1, Apr. 2, 1998.
Richelson et al., “Synthesis of a Potent Wide-spectrum Serotonin-, Norepnepherine- Dopamine-reuptake Inhibitor (SNDRI) and a Species-specific Dopamine-reuptake Inhibitor Based on the Gamma-amino Alcohol Functional Group.” Abstracts of Papers of the ACS 215: 154-Medi, Part 1, Apr. 2, 1998.
Richelson et al., “Development of Nonpeptidic Neurotensin (8-13) Mimetics.” Abstracts of Papers of the ACS 213: 61-Medi, Part 1, Apr. 13, 1998.
Richelson et al., “Development of a Neurotensin Agonist Crossing the Blood Brain Barrier,” Biol. Psychiatry 43, 49S, 1998.
Lindeberg, et al, Solid Phase Synthesis And Some Hormonal Activities of 1-Deamino-4-L-Valine-8-D-Homolysine- And 1-Deamino-4-L-Valine-8-D-Homoarginine-Vasapressin, Int. J. Peptide Protein Res. 10, 240-244, 1977.
Moore, et al., Effect of the basic amino-acid side chain length and the penultimate residue on the hydrolysis of benzoyldipeptides by carboxypeptidbase B1, Can. J. Biochem, 56, 315-318, 1978.
Nestor, et al., Potent, Long-Acting Luteinizing Hormone-Releasing Hormone Antagonists Containing New Synthetic Amino Acids: N,N′-Dialkyl-D-homoarginines1, J. Med. Chem, 31, 65-72, 1988.
Hilbert, et al., Design and Synthesis of Potent and Highly Selective Thrombin Inhibitors, J. Med. Chem. 37, 3889-3901, 1994.
U.S. patent application Ser. No. 10/043,581, Dix, filed Jan. 10, 2002.
Chebotareva et al. Lipoic Acid (6,8-Dithiooctanic Acid)—(II) Synthesis of Benzhydrylammonium Salts of DL-, &agr;.-Lipoyl-L-Phenylalanine, -L-Methionine, and -L-Valine.Chemical Abstracts Service, Database Accession No. CA62:7859a/AN, CAOLD, XP002194817, 62(7) (1965).
Havinga and Schattenkerk. Studies on Polypeptides—V1: Properties of the Arginyl Residue of Des-Asp1-IIe5-Angiotensin II Essential to Pressor Activity.Tetrahedron, 8(Part I):313-319 (1966).
Hempel and Lange. Synthese Tritium-markierter, N-methylierter Lysine.Hoppe-Seyler's Z. Physiol. Chem., 350:867-876 (1969).
Takahara et al. N&ohgr;-Dimethyl- or N&ohgr;-trimethyl-2,&ohgr;-diaminocarboxylic acids.6001 Chemical Abstracts, XP002194816, 69(25) (1968).
Kennedy et al. Asymmetric Synthesis of Non-Natural Homologues of Lysine.Bioorganic&Medical Chem. Ltrs., 7(14):1937-1940 (1997).
Kennedy et al. Design rationale, synthesis, and characterization of non-natural analogs of the cationic amino acids arginine and lysine.J. Peptide Res., 55(4):348-358 (2000).
Lundquist and Dix. Synthesis and Human Neurotensin Receptor Binding Activities of Neurotensin(8-13) Analogues Containing Position 8 &agr;-Azido-N-alkylated Derivatives of Ornithine, Lysine, and Homolysine.J. Med. Chem., 42:4914-4918 (1999).
Moore et al. N&egr;,N&egr;-Dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation.Biochem. J., 332:439-449 (1998).
Porcelli et al. A Kinetic Analysis of &ggr;-Aminobutyrate Aminotransferase in Presence and Absence of Inhibitors.Ber. Bunsenges. Phys. Chem., 100(5):671-679 (1996).
Takemoto et al. Hypotensive Constitutents of Marine Algae—(I) Basic Amino
Huff Sheela
Medical University of South Carolina Foundation Research Develop
Needle & Rosenberg P.C.
LandOfFree
Positively charged non-natural amino acids, methods of... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Positively charged non-natural amino acids, methods of..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Positively charged non-natural amino acids, methods of... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3084943