Inhibitors of β-lactamase

Details Inhibitors of β-lactamase Inhibitors of β-lactamase

2005-04-26

2005-04-26

Huang, Evelyn Mei (Department: 1625)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Phosphorus containing other than solely as part of an...

C514S272000, C514S301000, C514S307000, C514S311000, C514S314000, C514S333000, C514S335000, C514S342000, C514S343000, C514S351000, C514S363000, C514S367000, C514S309000, C514S374000, C514S338000, C514S378000, C514S389000, C514S397000, C514S418000, C514S422000, C514S428000, C514S443000, C514S445000, C514S468000, C514S470000, C514S473000, C514S604000, C514S092000, C514S096000, C514S117000, C546S022000, C546S023000, C546S024000, C546S025000, C548S112000, C548S113000

Reexamination Certificate

active

06884791

ABSTRACT:
The intention relates to bacterial antibiotic resistance and, in particular, to compositions and methods for overcoming bacterial antibiotic resistance. The invention provides novel β-lactamase inhibitors, which are structurally unrelated to the natural product and semi-synthetic β-lactamase inhibitors presently available, and which do not require a β-lactam pharmacophore. The invention also provides pharmaceutical compositions and methods for inhibiting bacterial growth.

REFERENCES:
patent: 3870771 (1975-03-01), Golburn et al.
patent: 3959551 (1976-05-01), Golburn et al.
patent: 4031170 (1977-06-01), Birum
patent: 4032601 (1977-06-01), Birum
patent: 5681821 (1997-10-01), Powers et al.
patent: 6075014 (2000-06-01), Weston et al.
patent: 6472406 (2002-10-01), Besterman et al.
patent: 2 261 081 (1972-12-01), None
patent: WO 9933850 (1999-07-01), None
patent: WO 00040030 (2000-01-01), None
patent: WO 0102411 (2001-01-01), None
Mikolajczyk, M., et al., Tetrahedron: Asymmetry (1997), 8(24), 3991-3994.*
Dai, Q and Chen, RY, Gaodeng Xuexia Huaxue Xuebao (1997), 18(12), 1992-1994.*
Chen, RY and Dai, Q Chin. Chem., Lett. (1955), 6(7), 561-564.*
Cremyln, et al., Phosphorus Sulfur (1979), 5(3), 277-86.
Cremlyn, et al., Phosphorus (1976), 6(3-4), 207-213.
Dryjanski, et al., “Inactivation of theEnterobacter cloacaeP99 β-Lactamase by a Fluorescent Phosphonate: Direct Detection of Ligand Binding at the Second Site,” Biochemistry, vol. 34, No. 11, 1995, pp. 3569-3575.
Li, et al., “Structure-Activity Studies of the Inhibition of Serine .beta.-Lactamases by Phosphonate Monoesters,” Bioorganic & Medicinal Chemistry, vol. 5, No. 9, 1997, pp. 1783-1788.
Jackson, et al., “Synthesis and Evaluation of Diphenyl Phosphonate Esters as Inhibitors of the Trypsin-like Granzyms A and K and Mast Cell Tryptase,” Journal of Medicinal Chemistry, vol. 41, No. 13, pp. 2289-2301.
Chen, et al., “The Synthesis of Novel Phosphonodipeptides and Their Herbicidal Activity”, Heteroatom Chemistry, vol. 4, No. 1, pp. 1-5.
Chen, “Study on the Mannich-Type Reaction of P-Toluenesulfonamide,” Chinese Chemical Letters, vol. 6, No. 3, pp. 181-184.
Rahil, J. and Pratt, RF, “Phosphate Monoester Inhibitors of class A β-lactamases,” Biochem. J. (1991) 275, 793-795.
Chen, et al., “Structure of a Phosphonate-inhibited β-Lactamase: An Analog of the Tectrahedral Transistion State/Intermediate of β-Lactam Hydrolysis,” J. Mol. Biol. (1993) 234, 165-178.
Maveyraud, et al., “Crystal Structure of an Acylation Transition-State Analog of the TEM-1 β-Lactamase, Mechanistic Implications for Class A β-Lactamases,” Biochemistry, 1998, 37, 2622-2628.
Rahil, J. and Pratt, RF, “Characterization of Covalently Bound Enzyme Inhibitors as Transition-State Analogs by Protein Stability Measurements: Phosphate Monoester Inhibitors of a β-Lactamase” Biochemistry, vol. 33, No. 1, 1994.
Rahil, J. and Pratt, RF, “Kinetics and Mechanism of β-Lactamase Inhibition by Phosphonamidates: The Quest for a Proton”, Biochemistry, vol. 32, No. 40, 1993.
Bateson, et al., “The Synthesis and Serine β-Lactamase Inhibitory Activity of Some Phosphonamidate Analogues of Dipeptides,” Bioorganic & Medi. Chemsitry Letters, vol. 4, No. 14, pp. 1667-1672, 1994.
Pratt, RF, “Inhibition of a Class C β-Lactamase by a Specific Phosphonate Monoester,” Nov. 17, 1989, vol. 246, pp. 917-919.
Rahil, J. and Pratt, RF, “Mechanism of Inhibition of the Class C β-Lactamase ofEnterobacter cloacaeP99 by Phosphonate Monoesters,” Biochemistry, vol. 31, No. 25, 1992.
Rahil, J., and Pratt, RF, Characterization of Covalently Bound Enzyme Inhibitors as Transition-State Analogs by Protein Stability Measurements: Phosphate Monoester Inhibitors of a β-Lactamase.
Rahil, J. and Pratt, RF, “Structure-Activity Relationships in the Inhibition of Serine β-Lactamases by Phosphonic Acid Derivatives,” Biochem pp. 389-393.
Silvaggi, et al., “The Crystal Structure of Phosphonate-Inhibited D-Ala-D-Ala Peptidase Reveals an Analogue of a Tetrahedral Transition State,” Biochem (2003).
Lobkovsky, et al., “Crystallographic Structure of a Phosphonate Derivative of theEnterobacter cloacaeP99 Cephalosporinase: Mechanistic Interpretation of a β-Lactamase Transition-State Analog,” Biochemistry 1994, 33, 3462-6772.
Dryjanski, Marek and Pratt, RF, “Steady-State Kinetics of the Binding of β-Lactams and Penicilloates to the Second Binding Site of theEnterobacter cloacaeP99 β-Lactamase,” Biochemistry 1995, 34, 3561-3568.
Rahil, J. and Pratt, RF, Intramolecular Participation of the Amide Group in Acid-and-Base-Catalysed Phosphonate Monoester Hydrolysis.
Xie, Gui-Yang et al., “Synthesis of a Novel Antigen Containing Phosphorus”, Chemical Journal of Chinese Universities, Gaodeng Xuexiao Huaxue Xuebao, vol. 24, No. 6, 2003, pp. 1037-1039.
Maveyraud, Laurent et al., “Crystal Structure of an Acylation Transition-State Analog of the TEM-1 β-Lactamase. Mechanistic Implications for Class A β-Lactamases”, Biochemistry, vol. 37, 1998, pp. 2622-2628.
Li, Naixin et al., “Structure-Activity Studies of the Inhibition of Serine β-Lactamases by Phosphonate Monoesters”, Bioorganic & Medicinal Chemistry, vol. 5, No. 9, pp. 1783-1788.
Chen, Celia C. H., et al., “Structure of a Phosphanate-Inhibited β-Lactamase. An Analog of the Tetrahedral Transition State/Intermediate of β-Lactam Hydrolysis”, Journal of Molecular Biology, vol. 234, pp. 165-178.
Rahil, Jubrail et al., “Characterization of Covalently Bound Enzyme Inhibitors as Transition-State Analogs by Protein Stability Measurements: Phosphonate Monoester Inhibitors of a β-Lactamase”, Biochemistry, vol. 33, 1994, pp. 116-125.
Rahil, Jubrail et al., “Structure-Activity Relationships in the Inhibition of Serine -β-Lactamases by Phosphonic Acid Derivitives”, Biochemical Journal, vol. 296, pp. 389-393.
Rahil, Jubrail et al., “Mechanism of Inhibition of the Class C β-Lactamase of Enterobacter Cloacae P99 by Phosphonate Monoesters”, Biochemistry, vol. 31, pp. 5869-5878.
Rahil, J. et al., “Intramolecular Participation of the Amide Group in Acid- and Base-Catalysed Phosphonate Monoester Hydrolysis”, Journal of the Chemical Society, Perkin Transactions 2: Physical Organic Chemistry, 1991, pp. 947-950.
International Search Report for PCT Application Ser. No. PCT/US03/36929, dated May 14, 2004.

Affiliated with

Also associated with

Rating

Inhibitors of β-lactamase does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Inhibitors of β-lactamase, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Inhibitors of β-lactamase will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3427111