Eureka AIR delivers breakthrough ideas for toughest innovation challenges, trusted by R&D personnel around the world.

Lysine compounds and their use in site- and chemoselective modification of peptides and proteins

A compound, lysine technology, applied in the field of lysine compounds and their use in site-selective and chemoselective modification of peptides and proteins, can solve the problems of lack of available and flexible methods, involvement, etc.

Inactive Publication Date: 2012-05-16
NETHERLANDS CANCER INST FOUNDATION
View PDF5 Cites 9 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0013] From the above it is evident that, while of particular interest in selectively modifying proteins, each of the currently available techniques suffers from specific drawbacks
There is often a great lack of available and flexible methods other than the described techniques

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
  • Lysine compounds and their use in site- and chemoselective modification of peptides and proteins
  • Lysine compounds and their use in site- and chemoselective modification of peptides and proteins
  • Lysine compounds and their use in site- and chemoselective modification of peptides and proteins

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0020] The first aspect of the present invention relates to the lysine compound represented by formula (Ia) or (Ib) or the ester, salt, solvate or hydrate of said lysine compound:

[0021]

[0022] Wherein -X- represents (i) sulfur or (ii) selenium; -P 1 and-P 2 independently represent (i) hydrogen or (ii) amine protecting group; -P 3 Represents (i) hydrogen; (ii) -X-R 6 The alkylthio, alkenylthio, alkylselenyl or alkenylselenyl shown, wherein -R 6 represents an optionally substituted branched or straight chain, aliphatic or cycloalkyl, heteroalkyl, alkenyl or heteroalkenyl moiety; (iii) a thiol or selenol protecting group; or (iv) -R 5 Part or (v) formula -C(=O)-R 5’ Part shown; -R 5 and -C(=O)-R 5’ represents the residue of a covalently bound ligand, preferably selected from peptides, lipids, carbohydrates, polymers, organic substances and inorganic substances; and -R 7 represents (i) hydrogen or (ii) optionally substituted branched or branched, aliphatic or cycloa...

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 present invention concerns new thiolysine and selenolysine compounds that can be used as building blocks for peptides and proteins, providing ligation handles for site-and chemoselective modification of said peptides and proteins. In particular, the invention provides. In particular, the invention provides (the use of) the compounds 5-thiolysine (also referred to as d-thiolysine); 4-thiolysine (also referred to as ?-thiolysine); 5-selenolysine (also referred to as d-selenolysine) and 4- selenolysine (also referred to as ?-selenolysine).; The positioning of the thiol or selenol group at the respective carbon atom allows for a very efficient intramolecular transfer reaction to take place after conjugation with a selected ligand, and the thiol or selenol group may subsequently be removed using reported procedures, thereby restoring the native lysine structure, or be used as an additional conjugation handle. The methodology is fast and gives well-defined material.

Description

technical field [0001] The present invention relates to the site-selective and chemoselective modification of peptides and proteins. In particular, the present invention provides novel thiolysine and selenolysine compounds useful as building blocks of said peptides and proteins. The lysine residue thus included can then serve as a target site for conjugation to a functional substance which is then typically transferred to the epsilon or alpha amine of the thio- or selenolysine residue. The invention also relates to these methods of site-selective and chemoselective modification of selected peptide or protein sequences, as well as to the intermediates and final products obtained in the respective steps of these methods. Background technique [0002] Covalent site-specific modification of proteins is a critical process in biological systems. Enzymatic modifications such as phosphorylation, glycosylation, sulfation, acetylation, methylation, ubiquitination, , Prenylation, SU...

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 Applications(China)
IPC IPC(8): C07C271/22A61K31/198C07C323/59C07C391/00C07K1/13
CPCC07C323/59C07C391/00C07K1/02C07C2103/18C07C271/22C07C2603/18A61K38/02
Inventor H·奥瓦F·埃尔瓦利德
Owner NETHERLANDS CANCER INST FOUNDATION
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
Eureka Blog
Learn More
PatSnap group products