The amino acid modification platform of BOC Sciences has accumulated many years of project synthesis, and has high-quality and cost-effective phosphorylated amino acids and peptides. The amino acid phosphorylation modification services we provide include O-phosphorylation, N-phosphorylation, S-phosphorylation and acyl phosphorylation.
Many proteins undergo different modifications on different groups after translation, such as glycosylation, methylation, acetylation, phosphorylation, etc. Among them, phosphorylation is the most common and important modification method after protein translation. This process is catalyzed by protein kinase to transfer the γ-position phosphate group of ATP or GTP to the amino acid residues (such as serine, threonine, tyrosine, etc.) of the substrate protein. Phosphorylation of proteins plays an important regulatory role in many biochemical processes (such as signal transduction, metabolic regulation, cell proliferation, etc.). Of the 20 natural amino acids, 9 (serine, threonine, tyrosine, histidine, lysine, arginine, cysteine, aspartic acid, and glutamic acid) can undergo phosphorylation modification.
Phosphorylated serine, phosphorylated threonine, and phosphorylated tyrosine play an important role in cell metabolism and regulation. Other phosphorylated amino acids cannot be ignored from a quantitative and functional point of view. Phosphorylated amino acids are the smallest molecular model of the chemical structure of phosphorylated proteins, which can be used in the modification of DNA, nucleosides and natural products, as well as in the synthesis of phosphopeptides, and have a wide range of applications in the fields of biotechnology, medicine, and pharmacy. Due to the various applications involving the structure of phosphorylated amino acids, we are committed to developing efficient methods for the synthesis of phosphorylated amino acids. Our high synthesis efficiency and cheap and easy-to-obtain raw materials are conducive to cost savings and efficient advancement of customer research projects.
The O-phosphorylation modification of amino acids refers to the process in which the side chain hydroxyl groups of amino acids are phosphorylated to generate phosphate esters. We commonly use the phosphoramidite triester method for the synthesis of O-phosphorylated amino acids. Based on trivalent phosphorus chemistry, this method is characterized by mild reaction conditions, high efficiency and high practicality, especially for the phosphorylation of serine, tyrosine, threonine and their derivatives.
N-phosphorylation is a phosphoramidite-type modification linked by a P(=O)-N bond, including phosphorylated histidine, lysine, and arginine. N-phosphorylated amino acid is a kind of non-esterified phosphate, and it is also a good phosphate group donor, which can form products such as peptides through intermolecular spontaneous reactions. We synthesize N-phosphorylated amino acids using various phosphorylating reagents (such as phosphorus oxychloride, dialkyl phosphate/carbon tetrachloride, dialkyl chlorophosphate, etc.).
S-phosphorylation is phosphorylation through the formation of P-S bonds between cysteine and phosphate groups.
Acyl phosphorylated amino acids are phosphorylated anhydrides formed by P-OCO bonds, including phosphorylated aspartic acid or glutamic acid.
Determination of phosphorylated amino acids is of great significance to the study of cell biology and biomedicine.