One of the most unresolved problems facing the scientific community is figuring out the function of post-translational modification patterns. Significant results from efforts to decipher the phosphorylation bio-barcode point to the possibility that many proteins actually exist in several versions, each with distinct phosphorylation patterns and roles. Peptide libraries make it relatively easy to simulate protein areas while studying highly phosphorylated regions is significantly more difficult. While practically universal techniques can be used to create basic phosphopeptides, the creation of phosphorylated peptide remains a significant synthetic problem. The insertion of multiple phosphate groups into different places on the peptide simultaneously or sequentially when there are numerous other potential modification sites is necessary for the synthesis of multiphosphopeptides.
These groups are heavy, unsteady, and difficult to introduce when they are near together. Furthermore, libraries made up of several peptides with varied levels and positions of phosphorylation are necessary if any methods have been discovered to enable the synthesis of phosphorylated peptides because the same protein region can have numerous alternative phosphorylated peptide patterns. These techniques are fundamentally distinct from those used to make straightforward phosphorylated peptides. We notably highlight the difficulties and significance of synthesizing phosphorylated peptide and their libraries. Modern approaches are given along with the historical viewpoint. The various synthetic strategies attempt to address the unique issues involved in the synthesis of multiphosphopeptides and offer a roadmap for the synthesis of such libraries.
Applications of the phosphorylated peptide
Creation of antibodies specific for the phosphorylation
For proteome identification, mass standards are developed
Development of assays using phosphatase substrates
Quantifying and Mapping sites of phosphorylation
Signal transduction and the cellular signaling pathways
The investigation of structural PTMs that control protein function.
Studying the roles that various disease like pathologies play, such as those in metabolic, neurodegenerative, and cancer.