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

Polypeptide sequence capable of specifically being bound to fumonisin B1 and applications thereof

A polypeptide sequence and fumonisin technology, applied in peptides, material inspection products, biological testing, etc., can solve the problems of peptides that have not been seen yet, and achieve easy mass preparation and purification, high affinity and specificity, and simple operation Effect

Active Publication Date: 2016-05-11
河南省农业科学院农业质量标准与检测技术研究所
View PDF1 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

But so far, has not yet seen the 1 Specifically binding polypeptides and applications thereof

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
  • Polypeptide sequence capable of specifically being bound to fumonisin B1 and applications thereof
  • Polypeptide sequence capable of specifically being bound to fumonisin B1 and applications thereof
  • Polypeptide sequence capable of specifically being bound to fumonisin B1 and applications thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0026] The present invention provides a combination with fumonisin B 1 A specifically binding polypeptide sequence, the polypeptide sequence is a phage display peptide, consisting of 12 amino acids, and the fumonisin B 1 There are five specific binding polypeptide sequences. Fumonisin B 1 There are five specific binding polypeptide sequences, the amino acid sequences of which are shown in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4 and SEQ ID NO: 5.

[0027] The nucleotide sequences corresponding to the five polypeptide sequences are shown in sequence as SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO:9 and SEQ ID NO:10.

[0028] To achieve the above object, the present invention adopts the following technical solutions:

[0029] A and fumonisin B 1 The specific binding polypeptide sequence, the method for preparing said polypeptide is as follows:

[0030] (1) Add FB 1 -BSA is coated on the microplate, and the plate is blocked with 5% BSA, and the phage displ...

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 discloses a polypeptide sequence capable of specifically being bound to fumonisin B1. The polypeptide sequence is five phage displaying peptides, which are composed of 12 amino acids. The provided phage displaying peptides, which can be bound to FB1, have high affinity and specificity to FB1; and compared with the conventional monoclonal antibody, the method of choosing phage displaying peptide that can be bound to target from a phage displaying random polypeptide library has the advantages of simple operation, and easiness for massive preparation and purification.

Description

technical field [0001] The invention belongs to the field of biotechnology, in particular to fumonisin B 1 Peptide sequence that specifically binds. The present invention provides energy and FB 1 Binding of phage-displayed peptides to FB 1 With high affinity and specificity, compared with traditional monoclonal antibodies, panning the phage display peptides that bind to the target from the phage display random peptide library has the characteristics of simple operation, easy mass preparation and purification. Background technique [0002] Fumonision (FumonisionFB) is a water-soluble secondary metabolite produced by Fusarium moniliforme Sheld and F.proliferatum under certain temperature and humidity conditions. It is a class of different polyhydric alcohols and tricarboxylic acids. Diester compounds with similar structures. Currently, the discovered fumonisins are FA 1 、FA 2 , FB 1 , FB 2 , FB 3 , FB 4 、FC 1 、FC 2 、FC 3 、FC 4 and FP 1 A total of 11 types, of wh...

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): C07K7/08G01N33/68
CPCC07K7/08G01N33/68
Inventor 刘冬梅刘继红尹海燕李淑芳曹成马莹贾斌周玲张迪孙江南任红
Owner 河南省农业科学院农业质量标准与检测技术研究所
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