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Cation amphiphilic membrane targeted alpha-helix polypeptides and application thereof

An amphiphilic membrane-targeted, cationic technology, applied in the direction of peptides, peptide/protein components, preparations for in vivo tests, etc., can solve problems such as difficult large-scale application, low yield, and complicated operation

Active Publication Date: 2015-10-14
SUZHOU INST OF NANO TECH & NANO BIONICS CHINESE ACEDEMY OF SCI
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, most of these peptides need to be extracted from organisms, the operation is complicated, the yield is low, and it is difficult to apply on a large scale

Method used

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  • Cation amphiphilic membrane targeted alpha-helix polypeptides and application thereof
  • Cation amphiphilic membrane targeted alpha-helix polypeptides and application thereof
  • Cation amphiphilic membrane targeted alpha-helix polypeptides and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0043] When X 1 is Arg, X 2 for Leu, X 3 When it is Ala, the polypeptide sequence (SEQ ID No.2, also referred to as sequence 2) is as follows: HGG-(RLARLAR) 2 -NH 2 .

[0044] 1. Key micelle concentration experiment of peptides

[0045] In the key micelle concentration experiment of the peptide, the peptide was diluted with Milli Q water, the concentration range was 1.56-300 μg / ml, and Nile Red was dissolved in dichloromethane to form a 500 micromolar solution, and 10 Microliter Nile Red, keep away from light to make dichloromethane evaporate to dryness, add 500 microliters of peptide solutions of various concentrations to the centrifuge tube containing Nile Red, keep away from light at 25 oC, shake overnight in a shaker at 250 rpm, use 485 nm excitation, fluorescence spectrometer to measure the fluorescence intensity of Nile Red at each concentration. Figure 2A The key micelle concentration curve of polypeptide sequence 2 is shown.

[0046] 2. Membrane-targeted local...

Embodiment 2

[0049] When X 1 is Arg, X 2 for Leu, X 3 When it is Leu, the polypeptide sequence (SEQ ID No.5, also referred to as sequence 5) is as follows: HGG-(RLRLLR) 2 -NH 2 .

[0050] 1. The key micelle concentration experiment of polypeptide

[0051] In the key micelle concentration experiment of the peptide, the peptide was diluted with Milli Q water, the concentration range was 1.56-300 μg / ml, and Nile Red was dissolved in dichloromethane to form a 500 micromolar solution, and 10 Microliter Nile Red, keep away from light to make dichloromethane evaporate to dryness, add 500 microliters of peptide solutions of various concentrations to the centrifuge tube containing Nile Red, keep away from light at 25 oC, shake overnight in a shaker at 250 rpm, use 485 nm excitation, fluorescence spectrometer to measure the fluorescence intensity of Nile Red at each concentration. Figure 2B The concentration change curve of the key micelle concentration of polypeptide sequence 5 is shown.

...

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Abstract

The invention discloses cation amphiphilic membrane targeted alpha-helix polypeptides and an application thereof. The polypeptides comprise an amino acid sequence [X1X2X3X1X2X3X1]n-NH2, wherein NH2 represents amination of C terminal; X1 is polar amino acid with positive charges; X2 and X3 are nonpolar hydrophobic amino acids; n is a positive integer; and all amino acids are L type amino acids. According to the invention, a series of cation amphiphilic membrane targeted alpha-helix polypeptides are provided, and have anti-cancer activity; different types of hydrophobic amino acids (L, I, F, A and the like) are remarkably different in the membrane action effect; and if the concentration is higher than the key micelle forming concentration, the hydrophobic amino acids can be self-assembled into a micro-micelle to generate a violent cell killing effect, and a new basis is provided for the development of anti-cancer drugs.

Description

technical field [0001] The invention specifically relates to the sequence design of a cationic amphiphilic membrane-targeted α-helix polypeptide and its application in cell tracking, cancer treatment and the like. Background technique [0002] Biomass membranes contain phospholipid components, so they have hydrophobic properties; related studies have shown that cancer cells have lower surface potentials than normal cells, showing stronger negative charges; mitochondria and nuclei also maintain strong internal negative potentials, so they are Ideal selective targets for cationic peptides. Peptide molecules have the advantages of good biocompatibility, multifunctionality and high diversity in structural design, which have aroused the interest of researchers. There are more and more researches on cationic amphipathic peptides in the field of cancer therapy, such as Xenobamadin and melittin. However, most of these peptides need to be extracted from organisms, the operation is ...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K7/08A61K38/10A61K49/00A61P35/00G01N33/68
Inventor 费浩曹睿马晓川贾俊丽
Owner SUZHOU INST OF NANO TECH & NANO BIONICS CHINESE ACEDEMY OF SCI
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