Ubiquitination is a reaction in which ubiquitin proteins are added to a substrate protein by the action of ubiquitin ligases. The ubiquitinated protein is recognized by the proteasome and undergoes proteolysis.
In recent years, research in medicinal chemistry has increasingly investigated the use of the ubiquitin-proteasome system (UPS) to combat diseases. As a result, a variety of chimera compounds have been synthesized consisting of a tag that can bind to ubiquitin ligase, a linker and another ligand that can bind to disease related proteins. This enables us to bring the disease related protein in proximity to an activated UPS to eliminate the protein.1)
Measuring the activity of these compounds has shown that the length of the linker is an important factor in triggering ubiquination.2) TCI now offers hetero-bifunctional linkers with a variety of lengths. We are also open to inquiries regarding scale up and custom synthesis of linkers and ligands. Please contact us for more information.
- Amino-PEG1-acid tert-Butyl Ester
- Amino-PEG2-acid tert-Butyl Ester
- Amino-PEG3-acid tert-Butyl Ester
- Amino-PEG4-acid tert-Butyl Ester
- (Boc-amino)-PEG1-carboxylic Acid
- (Boc-amino)-PEG2-carboxylic Acid
- (Boc-amino)-PEG3-carboxylic Acid
- (Boc-amino)-PEG4-carboxylic Acid
- 1) Chemical approaches to targeted protein degradation through modulation of the ubiquitin-proteasome pathway
- 2) Delineating the role of cooperativity in the design of potent PROTACs for BTK