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Pancreatic cancer specific binding peptide, preparation method and use thereof

A specific binding, pancreatic cancer technology, applied in the biological field, can solve the problems of large individual differences in therapeutic effects, high manufacturing costs, and high production costs, and achieve the effects of simple synthesis and purification, good effect, and weak immunogenicity.

Active Publication Date: 2019-10-15
中国医科大学
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

In addition, the existing anti-tumor drugs have strong toxicity and side effects during the treatment process due to their weak targeting, large individual differences in treatment effects, and high production costs.
Although most peptide drugs have strong anti-tumor targeting and rapid development, they still have problems such as high manufacturing costs and low yields.

Method used

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  • Pancreatic cancer specific binding peptide, preparation method and use thereof
  • Pancreatic cancer specific binding peptide, preparation method and use thereof
  • Pancreatic cancer specific binding peptide, preparation method and use thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0053] Example 1 Three rounds of subtractive screening of pancreatic cancer cell specific binding positive polypeptides using phage display technology

[0054] 1.1 Recovery and cultivation of host bacteria E.coli ER2738

[0055] To prepare an E. coli plate, take the LB-TET culture plate and preheat it in a 37-degree incubator for 1 hour. After the E.coli ER2738 bacterial liquid melts, use an inoculation loop to dip a small amount of bacterial liquid evenly on the culture plate, and then place it upside down at 37°C overnight in a constant temperature incubator. Prepare the host bacterial solution, pick a single colony from a well-grown culture plate, place it in LB bacterial culture solution containing tetracycline, and cultivate overnight at 37°C with shaking at 180rpm, so that the bacteria are in the logarithmic growth phase. The prepared LB-Tet plate containing Escherichia coli was stored in a 4°C refrigerator for later use, and the host bacterial solution was stored in a ...

Embodiment 2

[0079] Example 2 Determination and Analysis of DNA Sequence of Positive Phage Clones and Cell Immunohistochemical Identification of Targeted Binding Ability of Positive Phage Clones to Pancreatic Cancer Cells

[0080] 2.1 Determination and analysis of positive phage clone DNA sequence

[0081] 2.1.1 Positive monoclonal phage selection

[0082] The phage liquid obtained after the third round of screening was titered and spread on LB plates, and on the plates with less than 100 growing spots, 44 well-growing blue spots at an interval of 5 mm were randomly selected. Add 44 randomly picked coeruleus into 1 ml pre-logarithmic host bacterial solution (same as phage amplification), and amplify at 37°C and 200 rpm for 4.5 hours with rapid shaking.

[0083] 2.1.2 Positive monoclonal phage single-stranded DNA extraction

[0084] Centrifuge the amplified monoclonal phage liquid at 4°C and 14000rpm for 30 seconds, transfer the supernatant to a new tube, centrifuge at 4°C and 1000rpm for...

Embodiment 3

[0094] Example 3 Solid-phase synthesis of polypeptides and FITC-positive polypeptide fragments thereof

[0095] According to the measured amino acid sequence, the homology comparison analysis of its amino acid sequence and the bioinformatics analysis of its nucleic acid sequence are carried out. Polypeptide FY-YR (sequence is FYSHSNLNLKYR), FH-YN (sequence is FHLYLRYNLKYN), AD-YR (sequence is ADARYKSNLKYR), FH-YR (sequence is FHLFFLCRGDYR), DY-YN (sequence is DYHDPNLPTDYN ) by solid phase synthesis ) and FITC-positive polypeptide fragments FITC-FY-YR (sequence is FYSHSNLNLKYR), FITC-FH-YN (sequence is FHLYLRYNLKYN), FITC-AD-YR (sequence is ADARYKSNLKYR), FITC-FH-YR (sequence is FHLFFLCRGDYR) , FITC-DY-YN (sequence is DYHDPNLPTDYN), and identify the synthesized polypeptide. At the same time, the above polypeptides and FITC-positive polypeptide fragments were synthesized at Sangon Bioengineering (Shanghai) Co., Ltd.

[0096] 3.1 Preparation method of polypeptide FY-YR

[0097...

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Abstract

The present invention relates to a pancreatic cancer specific binding peptide, and a preparation method and a use thereof. The polypeptide is represented by the following general formula: X<1>X<2>X<3>X<4>X<5>X<6>X<7>X<8>X<9>X<10>YX<11>. The present invention also relates to the polypeptide, a bivalent body or a multivalent body formed thereof, a pharmaceutical composition of the targeting polypeptides and a preparation and an imaging preparation capable of killing cancer cells, and the use thereof. The polypeptide has a specific targeting effect on the pancreatic cancer cells, has strong selectivity, can be prepared by using a chemical synthesis method, and is high in purity, small in molecular weight, strong in specificity, free of immunogenicity and safe and reliable.

Description

technical field [0001] The invention relates to the field of biotechnology, in particular to a polypeptide (sequence X 1 x 2 x 3 x 4 x 5 x 6 x 7 x 8 x 9 x 10 YX 11 ) and its application with good binding specificity and sensitivity to human pancreatic cancer cells and tissues. Background technique [0002] Pancreatic cancer is the fourth leading cause of cancer death and has the lowest relative survival rate among all cancers. Its surgical resection rate is low, prognosis is poor, and mortality rate is high. For many years, the treatment of pancreatic cancer has not progressed, which is also one of the important reasons for the poor prognosis of patients. "Cancer Statistics, 2019" shows that the "five-year survival rate" of pancreatic cancer is only 9.3%, and it will become the second most deadly cancer by 2030. The main reason is that the clinical symptoms of pancreatic cancer are vague, lack of specific biomarkers, and it is difficult to be diagnosed. Once disc...

Claims

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Application Information

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IPC IPC(8): C07K7/08C07K1/06C07K1/04C12N15/11A61K47/64A61K45/00A61K51/08A61P35/00
CPCC07K7/08A61K47/64A61K45/00A61K51/08A61P35/00
Inventor 魏敏杰马赫遥范悦刘芳晓
Owner 中国医科大学
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