Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2005-08-23
2005-08-23
Weber, Jon (Department: 1653)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C514S002600, C514S003100, C514S012200, C514S013800, C514S014800, C514S021800, C530S350000, C530S323000, C530S324000, C530S325000, C530S326000, C530S327000, C424S464000
Reexamination Certificate
active
06933272
ABSTRACT:
The present invention relates to the use of at least a non-peptidyl compound as a biological modulator of insulin activity or insulin-related activity, which compound possesses ionic and hydrophobic chemical moieties spatially located so as to mimic at least an ionic and hydrophobic amino acid residue of insulin, which amino acids are associated with the binding of insulin to its receptor.
REFERENCES:
patent: 4871739 (1989-10-01), Baldwin et al.
patent: 4992418 (1991-02-01), Katsoyannis et al.
patent: 5008241 (1991-04-01), Markussen et al.
patent: 5149777 (1992-09-01), Hansen et al.
patent: 5175145 (1992-12-01), Cooper
patent: 5227466 (1993-07-01), DeMeyts
patent: 5514646 (1996-05-01), Chance et al.
patent: 5599841 (1997-02-01), Meglasson
patent: 5618913 (1997-04-01), Brange et al.
patent: 5629319 (1997-05-01), Luo et al.
patent: 5641796 (1997-06-01), Dominianni et al.
patent: 5652221 (1997-07-01), Larner et al.
patent: 5656722 (1997-08-01), Dorschug
patent: 5661168 (1997-08-01), Panetta et al.
patent: 5674900 (1997-10-01), Ubillas et al.
patent: 5686411 (1997-11-01), Gaeta et al.
patent: 5691386 (1997-11-01), Inman et al.
patent: 5693609 (1997-12-01), Baker et al.
patent: 5698669 (1997-12-01), Hoffmann et al.
patent: 5716927 (1998-02-01), Balschmidt et al.
patent: 5716975 (1998-02-01), Bue-Valleskey et al.
patent: 5817684 (1998-10-01), Fleisch et al.
patent: 5851988 (1998-12-01), Sportman et al.
patent: 6329431 (2001-12-01), Sportman et al.
patent: A 54495/86 (1986-09-01), None
patent: A 62066/86 (1987-03-01), None
patent: 0 325 224 (1989-07-01), None
patent: 0 433 225 (1991-06-01), None
patent: 0 618 227 (1994-10-01), None
patent: 0 132 366 (1995-01-01), None
patent: 2 037 002 (1970-12-01), None
patent: 1 305097 (1989-12-01), None
patent: WO 88/06599 (1988-09-01), None
patent: WO 90/01038 (1990-02-01), None
patent: WO 90/07522 (1990-07-01), None
patent: WO 90/12814 (1990-11-01), None
patent: WO 90 15816 (1990-12-01), None
patent: WO 95/17183 (1995-06-01), None
patent: WO 96/13613 (1996-05-01), None
patent: WO 97/27847 (1997-08-01), None
patent: WO 97/40017 (1997-10-01), None
Journal of the Japan Diabetes Society, vol. 42, No. 6, p. 461-465, 1999, Azami et al.
Ganong, 1989 Review of Medical Physiology, 1989.
Bajaj et al.,Biochem. J., 238:345-351 (1986) “Coypu insulin—Primary structure, conformation and biological properties of a hystricomorph rodent insulin”.
Bao et al.,Proc. Nat'l Acad. Sci.(USA), 94:2975-2980 (Apr. 1997) “Crystal structure of desheptapeptide (B24-B30)insulin at 1.6 Å resolution: Implications for receptor binding”.
Blundell et al.,Biochem. J.,125(3):50P-51P (Dec. 1971) “The Structure and Biology of Insulin”.
Blundell et al.,Proc. Nat'l. Acad. Sci.(USA),75(1):180-184 (Jan. 1978) “Insulin-like growth factor: A model for tertiary structure accounting for immunoreactivity and receptor binding”.
Blundell et al.,Advances in Protein Chemistry: 26, XII+431P., Academic Press: New York, NY USA, London, England, pp. 279-403 (1972) “Insulin: The Structure in the Crystal and its Reflection in Chemistry and Biology”.
Chu et al.,Biochemistry 26:6966-6971 (1987) “Possible Involvement of the A20-A21Peptide Bond in the Expression of the Biological Activity of Insulin. 1. [21-Desasparagine, 20-cysteinamide-A]insulin and [21-Desasparagine, 20-cysteine isopropylamide-A]Insulin”.
Chu et al.,Biochemistry, 26:6972-6979 (1987) “Possible Involvement of the A20-A21Peptide Bond in the Expression of the Biological Activity of Insulin. 2. [21-Asperagine diethylamide-A]insulin”.
Chu et al.,Biochemistry, 26:6975-6979 (1987) “Possible Involvement of the A20-A21Peptide Bond in the Expression of the Biological Activity of Insulin. 3. [21-Desasparagine,20-cyteine ethylamide-A]insulin and [21-Desasparagine,20-cysteine 2-,2,2-trifluoroethylamide-a]insulin”.
Corin et al.,J. Biol. Chem., 257(1):104-110 (Jan. 10, 1982) “Insulin Receptors Convert to a Higher Affinity State Subsequent to Hormone Binding—A Two-State Model for the Insulin Receptor”.
De Meyts et al.,Biochem. Biophys. Res. Comm., 55(1): 154-161 (1973) “Insulin Interactions With Its Receptors: Experimental Evidence For Negative Cooperativity”.
De Meyts,Bull. Mem. Acad. R. Med. Belg., 149(3-4):181-194 (1994) Abstract Only in English “Insulin receptors and mechanism of action of insulin and of insulin-like growth factors”.
Djuric et al.,J. Med. Chem., 32(6):1145-1147 (Jun. 1989) “Communications to the Editor”.
Donner,Proc. Nat'l. Acad. Sci.(USA),77(6):3176-3180 (Jun. 1980) “Regulation of insulin binding to isolated hepatocytes: Correction of bound hormone fragments linearizes Scatchard plots”.
Donner et al.,J. Biol. Chem., 258(15):9413-9418 (1983) “Hormone-induced Conformational Changes in the Hepatic Insulin Receptor”.
Easter et al.,Hoppe-Seylers A. Physiol. Bd., 359:S.229-1236 (Sep. 1978) “Crystalline [A21-Desamido]Bovine Insulin”.
Ferderigos et al.,Int. J. Peptide Protein Res., 13:43-53 (1979) “[21—Arginine—A]Insulin: A Biologically Active Analog”.
Gammeltoft,Physiol. Rev., 64(4):1321-1379 (Oct. 1984) “Insulin Receptors:Binding Kinetics and Structure-Function Relationship of Insulin”.
Gapinski et al.,J. Med. Chem., 33:2807-2813 (1990) “Benzophenone Dicarboxylic Acid Antagonists of Leukotriene B4. 2. Structure-Activity Relationships of the Lipophilic Side Chain”.
Garrett et al.,Nature, 394:395-399 (Jul. 23, 1998) “Crystal structure of the first three domains of the type-1 insulin -like growth factor receptor”.
Gattner et al.,Hoppe-Seyler's Z. Physiol. Chem. Bd., 358:S.105-112 (Jan. 1977) “[A21-Asparaginimide] Insulin—Saponification of Insulin Hexamethyl Ester, I”.
Hammond et al.,Am. J. Physiol, 272(6):1136-1144 (1997) “An Evaluation of the cross-linking model for insulin-receptor interactions”.
Harmon et al.,J. Biol. Chem., 258(11):6875-6881 (Jun. 10, 1983) “Characterization of a Membrane Regulator of Insulin Receptor Affinity”.
Harper et al.,J. Med. Chem., 37:2411-2420 (1994) “Leukotriene B4(LTB4) Receptor Antagonists: A Series of (Hydroxyphenyl)pyrazoles”.
Helmerhorst,Biochem. Biophys. Res. Commun., 147(1) 399-407 (Aug. 31, 1987) “The Insulin-Receptor Interaction: Is The Kinetic Approach For Inferring Negative-Cooperative Site-Site Interactions Valid?”.
Helmerhorst et al.,Biochem., 32(9):2356-2362 (1993) “Insulin Binding to Rat Liver Membranes Predicts a Homogeneous Class of Binding Sites in Different Affinity States That May Be Related to a Regulator of Insulin Binding”.
Hua et al.,Biochem., 30:5505-5515 (1991) “Comparative 2D-NMR Studies of Human Insulin and Des-pentapeptide Insulin: Sequential Resonance Assignment and Implications for Protein Dynamics and Receptor Recognition”.
Hua et al.,Nature, 354:238-240 (Nov. 21, 1991) “Receptor binding redefined by a structural switch in a mutant human insulin”.
Hua et al.,Biochem., 31:11940-11951 (1992) “Nonlocal Structural Perturbations in a Mutant Human Insulin Sequential Resonance Assignment and13C-Isotope-Aided 2D-NMR Studies of [PheB24-Gly]Insulin with Implications for Receptor Recognition”.
Hua et al.,Biochem., 32:1433-1442 (1993) “Dynamics of a Monomeric Insulin Analogue: Testing the Molten-Globule Hypothesis”.
Hubbard et al.,Nature, 372:746-755 (Dec. 22/29, 1994) “Crystal structure of the tyrosine kinase domain of the human insulin receptor”.
Hubbard,EMBO J., 16(18):5572-5581 (1997) “Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog”.
Isakoff et al.,Proc. Nat'l. Acad. Sci.(USA), 92:10247-10251 (Oct. 1995) “The inability of phosphatidylinositol 3-kinase activation to stimulate GLUT4 translocation indicates additional signaling pathways are requir
Helmerhorst Erik
Plewright Brian Scott
Marshall & Gerstein & Borun LLP
Robinson Hope A.
Weber Jon
LandOfFree
Use of non-peptidyl compounds for the treatment of insulin... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Use of non-peptidyl compounds for the treatment of insulin..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Use of non-peptidyl compounds for the treatment of insulin... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3506236