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Method for modifying protein tryptophan residues

A protein and tryptophan technology, applied in the field of biochemistry, can solve problems such as difficult modification of aromatic amino acids, and achieve remarkable technological progress

Pending Publication Date: 2022-04-01
SHENZHEN BAY LAB PINGSHAN TRANSLATIONAL MEDICINE CENT +2
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  • Abstract
  • Description
  • Claims
  • Application Information

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Problems solved by technology

[0004] The object of the present invention is to provide a method for modifying protein tryptophan residues, said method for modifying protein tryptophan residues should solve the problem that traditional protein amino acid probes in the prior art are difficult to modify aromatic amino acids question

Method used

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  • Method for modifying protein tryptophan residues
  • Method for modifying protein tryptophan residues
  • Method for modifying protein tryptophan residues

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Embodiment 1

[0031] 1. Synthesis of Thiol Substrates

[0032] 12.2 g of 4-hydroxybenzaldehyde and 11.8 g of propyne bromide were added to a round bottom flask and dissolved with 300 mL of ethanol. 13.8 g of anhydrous potassium carbonate was added to the reaction system, and heated under reflux in an oil bath for 6 hours. After the reaction, the organic solvent was removed by rotary evaporation, and 500 mL of water was added to dilute the obtained viscous mixture. The aqueous solution was extracted with 100 mL×3 ethyl acetate, the organic phases were combined, washed with 100 mL×2 0.1M dilute hydrochloric acid and 100 mL×2 saturated brine, dried over anhydrous sodium sulfate, and the organic solvent was removed by rotary evaporation. The crude product was recrystallized from petroleum ether and ethyl acetate, and the resulting white solid was filtered and dried, which was the product 4-propargyloxybenzaldehyde (13.9 g, yield 87%).

[0033] 1 H NMR (300MHz, Chloroform-d) δ9.84(s, 1H), 7.9...

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Abstract

The invention discloses a method for modifying protein tryptophan residues, which is used for chemically modifying the protein tryptophan residues through irradiation of visible light with proper wavelength in the presence of a photooxidation reduction catalyst by taking a thioacetal compound or a derivative thereof as a substrate. A nontoxic organic compound or a metal organic compound can be used as a catalyst, visible light is used as a light source, and the method is suitable for laboratory and industrial proteomics research and application.

Description

technical field [0001] The invention belongs to the field of biochemistry, and relates to a protein tryptophan probe, in particular to a method for modifying protein tryptophan residues. Background technique [0002] Trp is an ideal residue for bioconjugation because it is a rare (approximately 1% natural abundance) amino acid. It plays many important roles in protein function and has attracted increasing attention in recent years, but there is no robust modification method for tryptophan residues. [0003] Molecules such as sulfonium salts and sulfonium salts containing tetravalent organic sulfur (IV) are very practical active functional groups in organic chemical synthesis. The sulfonium salt intermediate formed by the photocatalytic desulfurization of thioacetal can interact with the electron-rich indole ring for S N Ar reacts to modify the side chain of tryptophan residues. It can solve the problem that traditional protein amino acid probes are difficult to modify aro...

Claims

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Application Information

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IPC IPC(8): C07K1/107C07K14/765
Inventor 李子刚尹丰王跃娜万川孔凌微
Owner SHENZHEN BAY LAB PINGSHAN TRANSLATIONAL MEDICINE CENT
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