A histone acetyltransferase chrono-current sensor based on gold-palladium nanoflowers/graphene composite and its application

An acetyltransferase and current sensor technology, applied in the field of functional biological materials and biosensing, to achieve high-sensitivity detection, fast detection speed, and good selectivity.

Active Publication Date: 2021-11-02
NINGBO UNIV
View PDF6 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

At present, there are no related reports on the preparation and application of histone acetyltransferase timing-current sensors based on gold-palladium nanoflowers / graphene composites at home and abroad

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
  • A histone acetyltransferase chrono-current sensor based on gold-palladium nanoflowers/graphene composite and its application
  • A histone acetyltransferase chrono-current sensor based on gold-palladium nanoflowers/graphene composite and its application
  • A histone acetyltransferase chrono-current sensor based on gold-palladium nanoflowers/graphene composite and its application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0031] Embodiment 1 Preparation of sensor

[0032](1) Acetyl antibody-gold palladium nanoflower / graphene composite material (Ab Ac - Preparation of AuPd@GO)

[0033] Disperse 0.5g graphene (GO) in 20mL deionized water and sonicate for 0.5h, then add 2.5mL 1g / L chloroauric acid (HAuCl 4 ) solution and 2.5mL 1g / L of chloropalladium acid (H 2 PdCl 4 ) solution, stirred evenly by magnetic force for 0.5h, placed under xenon arc lamp irradiation for 0.5h, then transferred to a drying oven, and reacted at 60°C for 24h. Finally, the sample was placed in a hydrogen tube furnace at 300 °C for 2 h. Disperse the prepared AuPd@GO in deionized water to obtain a 1 mg / mL AuPd@GO dispersion for later use.

[0034] Take 100 μL 1g / L acetyl antibody (Ab Ac ) placed in a He-Ne laser therapeutic apparatus for 30s irradiation, then added to 1mL of the above-mentioned AuPd@GO dispersion, and reacted at 37°C for 4h.

[0035] (2) Preparation of histone acetyltransferase timing-amperometric senso...

Embodiment 2

[0043] Example 2 Electrochemical response with or without p300

[0044] The histone acetyltransferase chrono-current sensor based on the gold-palladium nanoflower / graphene composite material and its application, using Example 1 to prepare our biosensor to explore the detection of histone acetyltransferase. See figure 2 , In the absence of p300, the sensor has basically no electrochemical response in PBS (0.1M, pH 7.0), while in the presence of p300, there is an obvious electrochemical response, which proves that the sensor can be used for p300 activity detection.

Embodiment 3

[0045] Example 3 Detection of p300 activity

[0046] Histone acetyltransferase timing-current sensor based on gold-palladium nanoflower / graphene composite material and its application, the preparation steps of the sensor are the same as in Example 1, during the acetylation reaction, the concentration of p300 and the concentration of p300 are changed successively For: 0, 0.001, 0.005, 0.01, 0.02, 0.05, 0.1, 0.2, 0.5, 1, 2, 5, 10, 20, 50, 100, 150, 200, 300, 500, 700, 1000 nM, subsequently used in the preparation sensor. Record the electrochemical response of the sensor in PBS (0.1M, pH 7.0). According to the experimental results, a series of electrochemical response curves corresponding to different concentrations of p300 are obtained, and the quantitative relationship between the electrochemical response current and the concentration of p300 is established. The quantitative relationship between the two determines the concentration of p300 in the sample to be tested. Experime...

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

PropertyMeasurementUnit
diameteraaaaaaaaaa
Login to view more

Abstract

The invention discloses a time-current sensor of histone acetyltransferase based on gold-palladium nanoflower / graphene composite material and its application. First, a substrate polypeptide is fixed on the surface of a gold electrode by the action of Au-S, and the acetylated The acetyl group on the coenzyme A is transferred to the specific lysine residue of the substrate polypeptide, and the acetylated antibody-gold palladium nanoflower / graphene composite material with strong catalytic ability is specifically adsorbed by the generated acetylated polypeptide, A distinct electrochemical signal is produced in an electrolyte solution containing hydrogen peroxide. In the acetylation reaction, the concentration of p300 and its small molecule inhibitor were changed, and the effects on the electrochemical signals of a series of sensors were explored through the specific binding of acetyl and acetyl antibodies. The advantages are good specificity, high sensitivity, fast detection speed, accurate and reliable results, and low cost.

Description

technical field [0001] The invention relates to a timing-current sensor and its application, in particular to an electrochemical detection method for histone acetyltransferase based on a gold-palladium nanoflower / graphene composite material, which belongs to the technical field of functional biological materials and biosensing. Background technique [0002] Post-translational modifications of histones, such as acetylation, phosphorylation, methylation, ADP-ribosylation, ubiquitination, etc., play an important role in the physiological and pathological processes of eukaryotic organisms. Among them, the acetylation of histone is mainly catalyzed by histone acetyltransferase (HAT), which uses acetyl-CoA as the reaction substrate to carry out enzymatic reaction, hydrolyzes the acetyl group on acetyl-CoA, and transfers it to histone On tail-specific lysine residues, this is a reversible process. p300 is a typical histone acetyltransferase, which has a wide range of biological fu...

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
Patent Type & Authority Patents(China)
IPC IPC(8): G01N27/26G01N27/327G01N33/543G01N33/573C01B32/182B82Y30/00B82Y15/00B01J23/52
CPCB01J23/52B01J35/0033B82Y15/00B82Y30/00C01B32/182G01N27/26G01N27/3278G01N33/5438G01N33/54386G01N33/573
Inventor 胡宇芳张青青胡丹丹郑宇迪冉平建刘鑫达郭智勇王邃晁多斌
Owner NINGBO UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap