Phosphorylation affects all aspects of cellular life, and protein kinases affect all aspects of intracellular communication functions by regulating signaling pathways and cellular processes. However, aberrant phosphorylation is also the cause of many diseases; in particular, mutated protein kinases and phosphatases can cause many diseases, and many natural toxins and pathogens also have an effect by altering the phosphorylation status of intracellular proteins.
Phosphorylation of serine (Ser), threonine (Thr), and tyrosine (Tyr) is a reversible protein modification process. They are involved in the regulation of many cellular activities, such as receptor signaling, protein association and segmentation, activation or inhibition of protein function, and even cell survival. Phosphates are negatively charged (two negative charges per phosphate group). Therefore, their addition alters the properties of the protein, which is usually a conformational change, leading to a change in the structure of the protein. When the phosphate group is removed, the conformation of the protein will return to its original state. If the two conformational proteins exhibit different activities, phosphorylation could act as a molecular switch for the protein to control its activity.
Many hormones regulate the activity of specific enzymes by increasing the phosphorylation state of serine (Ser) or threonine (Thr) residues, and tyrosine (Tyr) phosphorylation can be triggered by growth factors (such as insulin). The phosphate groups of these amino acids can be quickly removed. Thus, Ser, Thr, and Tyr functions as molecular switches in the regulation of cellular activities such as tumor proliferation.
Synthetic peptides play a very useful role in the study of protein kinase substrates and interactions. However, there are some factors that hinder or limit the adaptability of phosphopeptide synthesis technology, such as the inability to achieve full automation of solid-phase synthesis and the lack of convenient connection with standard analytical platforms.
The platform based peptide synthesis and phosphorylation modification technology overcomes these limitations while improving synthesis efficiency and scalability, and the platform is well suited for the study of protein kinase substrates, antigens, binding molecules, and inhibitors.
Post time: May-31-2023