Dipeptide ST with double functions of lowering blood pressure and lowering blood fat and application thereof

A lipid-lowering, dual-function technology applied in the field of active dipeptides

Inactive Publication Date: 2014-04-30
ZHEJIANG ACADEMY OF AGRICULTURE SCIENCES
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

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Problems solved by technology

[0019] According to existing drug reports, except for traditional Chinese medici

Method used

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  • Dipeptide ST with double functions of lowering blood pressure and lowering blood fat and application thereof
  • Dipeptide ST with double functions of lowering blood pressure and lowering blood fat and application thereof
  • Dipeptide ST with double functions of lowering blood pressure and lowering blood fat and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0058] 1) ACE inhibitory activity of dipeptide ST at a concentration of 1.0 mg / mL:

[0059] Chromatographic conditions: Solvent I is 0.05% trifluoroacetic acid (TFA) and 0.05% triethylamine (TTA) dissolved in deionized water (that is, every liter of solvent I contains 0.5mL of trifluoroacetic acid and 0.5mL of triethylamine ), solvent II is 100% chromatographically pure acetonitrile. The ratio of solvent Ⅰ to solvent Ⅱ is 70%: 30% (volume ratio), ultimate3000 Diane liquid chromatograph, and the chromatographic column is waters Symmetry C 18 5μm4.6×250mm, the flow rate is 0.5mL / min, the injection volume is 10μL, the detection wavelength is 225nm, and the detection column temperature is 30°C.

[0060] Detection method: The dipeptide ST obtained by chemical synthesis is tested for activity (the detection method is the same as above). At this time, the concentration of ST was 1.0 mg / mL.

[0061] Results: The ACE inhibitory activity of dipeptide ST at 1.0 mg / mL was 43.28%.

[0...

Embodiment 2

[0067] 1) ACE inhibitory activity of dipeptide ST at a concentration of 2.0 mg / mL:

[0068] Chromatographic conditions: solvent Ⅰ is 0.05% trifluoroacetic acid (TFA) and 0.05% triethylamine (TTA) dissolved in deionized water; solvent Ⅱ is 100% chromatographically pure acetonitrile. The ratio of solvent Ⅰ to solvent Ⅱ is 70%: 30%, the ultimate3000 Diane liquid chromatograph, the chromatographic column is waters Symmetry C 18 5μm4.6×250mm, the flow rate is 0.5mL / min, the injection volume is 10μL, the detection wavelength is 225nm, and the detection column temperature is 30°C.

[0069] Detection method: The dipeptide ST will be obtained through chemical synthesis for activity detection (the detection method is the same as above). At this time, the ST concentration was 2.0 mg / mL.

[0070] Results: The ACE inhibitory activity of dipeptide ST at 2.0 mg / mL was 67.45%.

[0071] 2) HMG-CoA reductase inhibitory activity of dipeptide ST at a concentration of 2.0 mg / mL:

[0072] Chrom...

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Abstract

The invention belongs to the technical field of biology, and particularly relates to a dipeptide capable of being combined with angiotensin converting enzyme to inhibit activity of the angiotensin converting enzyme and inhibit activity of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase. The invention particularly discloses a dipeptide ST with double functions of lowering blood pressure and lowering blood fat, wherein the amino acid sequence of the dipeptide ST is Ser-Thr. The invention also discloses application of the dipeptide ST in preparing ACE (angiotensin converting enzyme) inhibitory peptide and/or HMG-CoA reductase inhibitory peptide.

Description

technical field [0001] The invention belongs to the field of biotechnology, and particularly relates to an angiotensin-converting enzyme that can be combined to inhibit its activity, and can also inhibit the activity of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase of dipeptides. Background technique [0002] Angiotensin converting enzyme (Angiotensin converting enzyme, ACE, EC3.4.15.1, once used in the literature as kininaseIl, dipeptidyl carboxypeptidase I, etc.) is a dicarboxypeptidase, which is a key enzyme leading to high blood pressure. It passes Hydrolysis converts angiotensin I to angiotensin II, and at the same time, ACE can also inactivate bradykinin, both of which can lead to vasoconstriction and thus hypertension. Therefore, ACE is considered to be an important factor causing hypertension. Studies have found that angiotensin-converting enzyme inhibitors (ACEI) can lower blood pressure by inhibiting the activity of ACE. ACE inhibitors are widely use...

Claims

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Application Information

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IPC IPC(8): C07K5/062A61K38/05A61P9/12A61P3/06
Inventor 王伟王楠张玉杨玉英
Owner ZHEJIANG ACADEMY OF AGRICULTURE SCIENCES
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