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Compositions and methods for treating cardiovascular disease and myocardial infarction with dipeptidyl peptidase inhibitors or b type natriuretic peptide analogues resistant to prolyl-specific dipeptidyl degradation

a technology of dipeptides and analogues, which is applied in the field of medical diagnostics and therapeutics, to achieve the effects of improving diagnostic and prognostic information, good stability, and facilitating patient treatmen

Inactive Publication Date: 2015-10-22
ALERE SAN DIEGO INC
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

The patent text describes a method for designing an assay for detecting natriuretic peptides that are biologically active forms of the peptides, while also preventing the assay from detecting inactive fragments. The method takes into account the degradation of the peptides and the presence of carbohydrate residues that can affect the assay results. The technical effect of this method is improved accuracy and sensitivity in detecting the biologically active forms of the peptides, which can aid in the diagnosis and treatment of cardiovascular diseases. The patent also describes the use of inhibitors of prolyl-specific DPP, which can stabilize the peptides and improve their therapeutic potential. Additionally, the patent discusses the use of exogenously added natriuretic peptides and glycosylated forms of the peptides in the assay, which can further improve the detection of the peptides.

Problems solved by technology

Failure to consider this degradation when designing an assay for one or more natriuretic peptides may result in an assay that detects both biologically active forms of a natriuretic peptide(s) of interest, as well as inactive fragments of the natriuretic peptide(s).

Method used

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  • Compositions and methods for treating cardiovascular disease and myocardial infarction with dipeptidyl peptidase inhibitors or b type natriuretic peptide analogues resistant to prolyl-specific dipeptidyl degradation

Examples

Experimental program
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example 1

Blood Sampling

[0177]Blood is preferably collected by venous puncture using a 20 gauge multi-sample needle and evacuated tubes, although fingertip puncture, plantar surface puncture, earlobe puncture, etc., may suffice for small volumes. For whole blood collection, blood specimens are collected by trained study personnel in EDTA-containing blood collection tubes. For serum collection, blood specimens are collected by trained study personnel in thrombin-containing blood collection tubes. Blood is allowed to clot for 5-10 minutes, and serum is separated from insoluble material by centrifugation. For plasma collection, blood specimens are collected by trained study personnel in citrate-containing blood collection tubes and centrifuged for ≧12 minutes. Samples may be kept at 4° C. until use, or frozen at −20° C. or colder for longer term storage. Whole blood is preferably not frozen.

example 2

Recombinant Antibody Preparation

[0178]Immunization of Mice with Antigens and Purification of RNA from Mouse Spleens

[0179]Mice are immunized by the following method based on experience of the timing of spleen harvest for optimal recovery of mRNA coding for antibody. Two species of mice are used: Balb / c (Charles River Laboratories, Wilmington, Mass.) and A / J (Jackson Laboratories, Bar Harbor, Me.). Each of ten mice are immunized intraperitoneally with antigen using 50 μg protein in Freund's complete adjuvant on day 0, and day 28. Tests bleeds of mice are obtained through puncture of the retro-orbital sinus. If, by testing the titers, they are deemed high by ELISA using biotinylated antigen immobilized via streptavidin, the mice are boosted with 50 μg of protein on day 70, 71 and 72, with subsequent sacrifice and splenectomy on day 77. If titers of antibody are not deemed satisfactory, mice are boosted with 50 μg antigen on day 56 and a test bleed taken on day 63. If satisfactory titer...

example 3

Biochemical Analyses

[0222]BNP is measured using standard immunoassay techniques. These techniques involve the use of antibodies to specifically bind the protein targets. An antibody directed against BNP is biotinylated using N-hydroxysuccinimide biotin (NHS-biotin) at a ratio of about 5 NHS-biotin moieties per antibody. The biotinylated antibody is then added to wells of a standard avidin 384 well microtiter plate, and biotinylated antibody not bound to the plate is removed. This formed an anti-BNP solid phase in the microtiter plate. Another anti-BNP antibody is conjugated to alkaline phosphatase using standard techniques, using SMCC and SPDP (Pierce, Rockford, Ill.). The immunoassays are performed on a TECAN Genesis RSP 200 / 8 Workstation. Test samples (10 μL) are pipetted into the microtiter plate wells, and incubated for 60 min. The sample is then removed and the wells washed with a wash buffer, consisting of 20 mM borate (pH 7.42) containing 150 mM NaCl, 0.1% sodium azide, and 0...

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Abstract

The present invention describes compositions and methods for treating cardiovascular disease and myocardial infarction using dipeptidyl peptidase inhibitors. Also provided are methods for increasing natriuretic peptide function by administering one or more analogues of B type natriuretic peptide that provide increased stability in the presence of prolyl-specific dipeptidyl peptidases.

Description

CROSS-REFERENCE[0001]This application is a continuation of U.S. patent application Ser. No. 12 / 391,157, filed on Feb. 23, 2009, which is a continuation of U.S. patent application Ser. No. 11 / 560,425, filed Nov. 16, 2006, which is a continuation of U.S. patent application Ser. No. 10 / 938,760, filed Sep. 9, 2004, now U.S. Pat. No. 7,524,635; which claims the benefit of U.S. Provisional Application No. 60 / 542,086, filed Feb. 4, 2004, and which is a continuation-in-part of U.S. patent application Ser. No. 10 / 645,874, filed Aug. 20, 2003, and Ser. No. 10 / 419,059, filed Apr. 17, 2003, which is a continuation-in-part of U.S. patent application Ser. No. 09 / 835,298, filed Apr. 13, 2001, now U.S. Pat. No. 7,632,647, and Ser. No. 10 / 139,086, filed May 4, 2002, now U.S. Pat. No. 7,361,473, which claims the benefit of U.S. Provisional Application Nos. 60 / 315,642, filed Aug. 28, 2001, and 60 / 288,871, filed May 4, 2001; and U.S. patent application Ser. No. 10 / 419,059, filed Apr. 17, 2003, is a con...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): A61K38/05A61K45/06A61K38/22A61K39/395C07K16/40G01N33/53
CPCA61K38/05A61K45/06A61K38/2242A61K38/06C07K16/26G01N33/6893G01N33/74C07K2317/34A61P9/00A61K2300/00G01N33/5306G01N33/543G01N33/68G01N33/6827G01N2400/02G01N2440/38
Inventor WHITTAKER, MICHAEL A.
Owner ALERE SAN DIEGO INC
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