Administration of dipeptidyl peptidase inhibitors

a technology of dipeptidyl peptidase and inhibitor, which is applied in the direction of peptides, drug compositions, metabolic disorders, etc., can solve the problems of short half-life and rapid degradation of glp-1 (7-36)

Inactive Publication Date: 2007-03-15
TAKEDA PHARMA CO LTD
View PDF99 Cites 206 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0021] Combination of Compound I with one or more antidiabetic compounds other than Compound I provides excellent effects such as 1) enhancement in therapeutic effects of Compound I and / or the antidiabetic compounds; 2) reduction in side effects of Compound I and / or the antidiabetic compounds; and 3) reduction in a dose of Compound I and / or the antidiabetic compounds.
[0046] Combination of Compound I with one or more antidiabetic compounds other than Compound I provides excellent effects such as 1) enhancement in therapeutic effects of Compound I and / or the antidiabetic compounds; 2) reduction in side effects of Compound I and / or the antidiabetic compounds; and 3) reduction in a dose of Compound I and / or the antidiabetic compounds.

Problems solved by technology

Unfortunately, GLP-1 (7-36) is degraded rapidly in vivo and has been shown to have a short half-life in vivo (t1 / 2=1.5 minutes).

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Administration of dipeptidyl peptidase inhibitors
  • Administration of dipeptidyl peptidase inhibitors
  • Administration of dipeptidyl peptidase inhibitors

Examples

Experimental program
Comparison scheme
Effect test

examples

1. Preparation of 2-[6-(3-Amino-piperidin-1-yl)-3-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-ylmethyl]-4-fluoro-benzonitrile and Pharmaceutically Acceptable Salts

[0168]

[0169] A mixture of 2-bromo-5fluorotoluene (2) (3.5 g, 18.5 mmol) and CuCN (2 g, 22 mmol) in DMF (100 mL) was refluxed for 24 hours. The reaction was diluted with water and extracted with hexane. The organics were dried over MgSO4 and the solvent removed to give product 3 (yield 60%). 1H-NMR (400 MHz, CDCl3): δ 7.60 (dd, J=5.6, 8.8 Hz, 1H), 6.93-7.06 (m, 2H), 2.55 (s, 3H).

2-Bromomethyl-4-fluorobenzonitrile (4)

[0170] A mixture of 4-fluoro-2-methylbenzonitrile (3) (2 g, 14.8 mmol), NBS (2.64 g, 15 mmol) and AIBN (100 mg) in CCl4 was refluxed under nitrogen for 2 hours. The reaction was cooled to room temperature. The solid was removed by filtration. The organic solution was concentrated to give crude product as an oil, which was used in the next step without further purification. 1H-NMR (400 MHz, CDCl3): δ 7.68 (dd,...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

PropertyMeasurementUnit
timeaaaaaaaaaa
timeaaaaaaaaaa
molecular weightaaaaaaaaaa
Login to view more

Abstract

Pharmaceutical compositions comprising 2-[6-(3-Amino-piperidin-1-yl)-3-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-ylmethyl]-4-fluoro-benzonitrile and pharmaceutically acceptable salts thereof are provided as well as kits and articles of manufacture comprising the pharmaceutical compositions as well as methods of using the pharmaceutical compositions.

Description

RELATED APPLICATION [0001] This application claims the benefit of U.S. Provisional Application No. 60 / 717,560 filed Sep. 14, 2005 and U.S. Provisional Application No. 60 / 747,280 filed May 15, 2006, each of which is incorporated herein by reference.FIELD OF THE INVENTION [0002] The invention relates to the method of administering compounds used to inhibit dipeptidyl peptidase IV as well as treatment methods based on such administration. DESCRIPTION OF RELATED ART [0003] Dipeptidyl Peptidase IV (IUBMB Enzyme Nomenclature EC.3.4.14.5) is a type II membrane protein that has been referred to in the literature by a wide a variety of names including DPP4, DP4, DAP-IV, FAPβ, adenosine deaminase complexing protein 2, adenosine deaminase binding protein (ADAbp), dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidase; postproline dipeptidyl aminopeptidase IV; lymphocyte antigen CD26; glycoprotein GP110; dipeptidyl peptidase IV; glycylproline aminopeptidase; gl...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
Patent Type & Authority Applications(United States)
IPC IPC(8): A61K38/04A61K31/426
CPCA61K31/426A61K31/44A61K31/513A61K38/26A61K45/06Y10S514/866A61K2300/00A61K9/2018A61P3/00A61P31/18A61P35/00A61P43/00A61P5/50A61P3/10
Inventor CHRISTOPHER, RONALD J.COVINGTON, PAUL
Owner TAKEDA PHARMA CO LTD
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap