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

A method for enzyme-catalyzed selective amidation and hydrazide modification of polypeptide C-terminus

A C-terminal and hydrazide technology, which is applied in the field of enzyme-catalyzed selective amidation and hydrazide modification of polypeptide C-terminus, can solve the problems of low yield, high difficulty, and many chemical modification steps, and achieve substrate spectrum Broad, mild effect

Active Publication Date: 2022-05-06
INST OF MICROBIOLOGY - CHINESE ACAD OF SCI
View PDF0 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0003] Due to the complexity of the polypeptide structure, there are many chemical modification steps, low yield and great difficulty

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 method for enzyme-catalyzed selective amidation and hydrazide modification of polypeptide C-terminus
  • A method for enzyme-catalyzed selective amidation and hydrazide modification of polypeptide C-terminus
  • A method for enzyme-catalyzed selective amidation and hydrazide modification of polypeptide C-terminus

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0034] Example 1. Enzyme-catalyzed selective amidation and hydrazide modification of polypeptide C-terminus

[0035] In this example, the amino acid at position 1 of the C-terminus of the polypeptide is selectively amidated and hydrazidated using the polypeptide terminal amidation enzyme (PAM12B) shown in SEQ ID No.1.

[0036] Reaction process: The C-terminally amidated polypeptide to be modified is catalyzed by PAM12B shown in SEQ ID No.1 and nucleophilic organic amine (NH 2 R) reaction, thereby realizing the amidation and hydrazide modification of the C-terminal amino acid of the polypeptide to be modified.

[0037] Wherein, the general formula of the nucleophilic organic amine with the modifying group is NH 2 R can specifically be any of the following:

[0038]

[0039] 1. Preparation of polypeptide terminal amidation enzyme (PAM12B)

[0040] Adopt the double-stranded DNA molecule shown in SEQ ID No.2 (the coded gene of polypeptide end amidating enzyme PAM12B shown in...

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 an enzyme-catalyzed polypeptide C-terminal selective amidation and hydrazidation modification method. The present invention provides a method for amidation and / or hydrazidation modification of the C-terminal amino acid of a polypeptide, which uses a specific protein to amidate and / or hydrazidate the C-terminal amino acid of the polypeptide; the specific protein is SEQ The protein shown in ID No.1. This method can be used to achieve amidation and / or hydrazidation modification of the C-terminal amino acid of the polypeptide, and it is an aqueous reaction with mild conditions. The C-terminal is selectively modified without affecting other modification groups on the side chain, and the side chain does not need to be protected. , with a wide substrate spectrum and no restriction on the amino acid sequence of the substrate polypeptide. Any amino acid at the terminal end of the modified polypeptide can be modified except proline.

Description

technical field [0001] The invention relates to the field of polypeptide chemistry, in particular to an enzyme-catalyzed C-terminal selective amidation and hydrazide modification method of polypeptide. Background technique [0002] The terminal functionalization of a polypeptide has a very important impact on its biochemical properties. Through the specific modification of the C-terminus, the in vivo metabolic half-life of the polypeptide can be prolonged, and the immunogenicity or toxic side effects can be reduced. In the study of the biochemical properties of peptides, researchers often need to add different functional groups (for example, fluorescent groups, synthetic polymers or immunolabels) to the peptide structure. In addition, efficient and accurate peptide C-terminal protection, deprotection and selective activation methods are also urgently needed technologies in industrial peptide synthesis and production. Therefore, the selective C-terminal modification method ...

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): C12P21/00
CPCC12P21/00
Inventor 吴边李瑞峰田玉娥
Owner INST OF MICROBIOLOGY - CHINESE ACAD OF SCI
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