Phosphorylation is an important and reversible post-translational modification of peptides and proteins. This modification involves the addition of phosphate groups to amino acid residues in the peptide or protein, occurring primarily on the hydroxyl groups of the side chains of serine (Ser), tyrosine (Tyr), and threonine (Thr) residues. Phosphorylation modifications affect all aspects of cell life, including signal transduction, cell division, metabolism, and apoptosis. Alfa Chemistry has mature peptide phosphorylation modification technology and provides a variety of phosphorylation modification services. We have successfully delivered a large number of phosphopeptides to our customers.
Our Services
Relying on our own technical advantages, we provide L-type phosphorylation modification and D-type phosphorylation modification services, as detailed in the table below. In addition, we can perform phosphorylation modifications at one, two, three, four, or five sites at the same time.
Methods of Peptide Phosphorylation Modification
Currently, there are two main methods for phosphorylation modification of peptides.
- Introduce appropriately protected phosphorylated amino acids directly into the peptide sequence.
The amino acids (Ser, Tyr or Thr) that need to be phosphorylated are phosphorylated and appropriately protected in advance, and then the phosphorylated monomer is condensed to the designated site of the peptide according to the normal solid-phase peptide synthesis (SPPS) synthesis process. This method is easy to operate and has become the main method for single-site phosphorylation modification of peptides.
- After the peptide sequence is synthesized on the resin, the side chain hydroxyl group of Ser, Tyr or Thr is phosphorylated.
When phosphorylation modification is performed by condensing phosphorylated monomers into peptides, the phosphorylated amino acids are difficult to condense with the peptide chain due to the steric hindrance caused by the larger side chain modification groups, and the subsequent introduction of amino acids will be relatively difficult. Especially when it contains multiple phosphorylation modification sites, the synthesis will become extremely difficult, and the final product will have complex components, making it difficult to separate, and the yield will be extremely low. Therefore, when multiple sites in the peptide chain are phosphorylated, you can consider phosphorylating the side chain hydroxyl groups of Ser, Tyr or Thr after the peptide sequence is synthesized on the resin. The synthesis process is mainly to selectively remove the side chain protecting group of the amino acid to be modified after the peptide synthesis is completed, and then phosphorylate it. For Tyr and Thr, amino acids with unprotected side chains can be used directly for the reaction.
Applications of Phosphorylated Modified Peptides
- Biomarker discovery. Phosphorylated peptides can serve as biomarkers for disease diagnosis and prognosis. Monitoring changes in the phosphorylation status of specific peptides in biological samples can provide valuable information about disease progression and treatment response.
- Proteomics research. Phosphorylation is a common post-translational modification that regulates protein function. Studying phosphorylated peptides can provide insights into complex signaling networks and help elucidate the molecular mechanisms underlying various biological processes.
- Signal transduction research. Phosphorylation is a key mechanism of signal transduction in cells, regulating various cellular processes such as cell growth, differentiation, and apoptosis. Investigating the phosphorylation status of specific peptides can help in understanding how signaling pathways are modulated in response to external stimuli.
Service Process
