Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Recombinant octreotide and uses thereof

A technology of octreotide and nucleotide sequence, which is applied in the field of recombinant octreotide and its application, can solve the problems that can not be used to prepare drugs for targeted therapy, can not realize targeted brachytherapy of tumor cells, etc., and achieve fast blood clearance, Reagents are cheap and easy to obtain, and the method is simple

Inactive Publication Date: 2008-05-21
王自正 +4
View PDF0 Cites 5 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

but 99m Tc-Octreotide is only used for imaging and cannot achieve the purpose of targeted brachytherapy of tumor cells, so it cannot be used for the preparation of drugs for targeted therapy

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
  • Recombinant octreotide and uses thereof
  • Recombinant octreotide and uses thereof
  • Recombinant octreotide and uses thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0027] Embodiment 1: Preparation of recombinant Tyr-Octreotide

[0028] According to the provided sequence SEQ ID NO.2, it is well known to those skilled in the art to synthesize small molecule polypeptides by using known techniques. In the present invention, Tyr-Octreotide, which replaces phenylalanine with tyrosine, was researched by Beijing Huada Gene Prepared in the center, the prepared small molecular protein Tyr-Octreotide was analyzed by high-performance liquid chromatography (HPLC), and after molecular weight determination, it was the desired protein with a purity >95%. Sequencing analysis is SEQ ID NO.2.

Embodiment 2

[0029] Embodiment 2: preparation 131 I-Tyr-Octreotide

[0030] 131 Labeling of I-Tyr-Octreotide: take 0.2mol / L NaH 2 PO 4 and 0.2mol / L Na 2 HPO 4 Configured as 0.2mol / L PB; weigh 0.3g of Ch-T and Na 2 S 2 o 5 Prepare a reaction solution of 30 μg / μL; prepare Tyr-Octreotide with a concentration of 1 mg / ml. Take 150 μL of PB at 25°C, add Octreotide 10 μL, Na 131 I (0.15mCi) 0.1ml, Ch-T 4μL reaction 3min and shake quickly to mix, then add Na 2 S 2 o 5 5 μL, labeling conditions: ①The pH value of phosphate buffer is from 6.0 to 9.2; ②The amount of Tyr-Octreotide is 1 μg, 5 μg, 10 μg, 15 μg, 20 μg; ③Reaction temperature is 25°C, ④Reaction time is 2-3min. mark in minutes 131 I-Tyr-Octreotide.

[0031] Determination of prepared 131 The radiochemical purity and in vitro stability of I-Tyr-Octreotide: Two systems are used: System 1 uses Xinhua No. 1 chromatography paper as the stationary phase, and normal saline as the developer. 131 I-Tyr-Octreotide and colloid ratio shi...

Embodiment 3

[0033] Example 3: 131 Distribution of I-Tyr-Octreotide in normal mouse tissues

[0034] Thirty Kunming mice (20-25g) were randomly divided into 6 groups, 5 in each group. tail vein injection 131 I-Tyr-Octreotide 0.15mL (3.7MBq), imaging was carried out at 30min, 4, 8, 12, 24, 48h after administration, and then the mice were killed by taking blood from the eyeballs. Take important tissues and organs, including heart, liver, spleen, lung, kidney, stomach, small intestine (1cm away from the stomach), large intestine, pancreas, femur, muscle, brain, thyroid, etc. 13 tissues and organs, weigh and measure the radioactive count, calculate %ID / g (radioactive count per gram of tissue / total radioactive count injected into mice × 100%). The blood clearance curve was drawn with time as the abscissa and radioactive count as the ordinate, and was fitted with Origin5.0 software to calculate and analyze its pharmacokinetic parameters in normal mice.

[0035] After tail vein injection, its...

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

No PUM Login to View More

Abstract

The invention belongs to the biological engineering field and discloses a recombinant octreotide and an application thereof. Aiming at the problems that the prior octreotide can not realize targeting short-distance irradiation towards tumour cells and can not be applied to the preparation of targeting curative drug, the invention provides a recombinant octreotide, the amino acid sequence of which is shown as SEQ ID NO.2. The recombinant octreotide is in favor of radioactive isotope <131>I marking and can be applied to the preparations of antitumor drug or targeting diagnosis reagent.

Description

technical field [0001] The invention belongs to the field of bioengineering and relates to a recombinant octreotide and its application. Background technique [0002] Due to their strong receptor specificity, easy synthesis and modification, less immune response, easy tissue penetration and fast blood clearance, small molecular peptides have become a hot spot in nuclide-targeted diagnosis and treatment research in recent years. [1-3] . Somatostatin (SST) is a neuropeptide that circulates in the body, and it acts as a brain neurotransmitter that can inhibit the release of various hormones [4-5] , such as growth hormone, insulin, glucagon, gastrin, etc. Somatostatin and its analogues are a relatively mature small molecule polypeptide used so far, which can inhibit cell proliferation by resisting signal transduction. Octreotide is an analogue of somatostatin, which is a natural somatostatin molecule. Modified artificially synthesized 8-peptide, which has the function of inhi...

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
IPC IPC(8): C07K7/06C07H21/04A61K38/08A61K51/08A61P35/00A61K101/02
Inventor 王自正王峰杜同信李少华瞿卫
Owner 王自正
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com