Peptides: It is used to prepare map antibody epitopes, epitope-specific antibodies and enzyme biding sides and also to design drugs, enzymes, and vaccines. Peptide synthesis used to be labor-intension and produce low yields. It is also used to improve methods of production and peptide chemistry.

Introduction to peptide synthesis:

It is characterized as the formation of the peptide bond between two amino acids and it is usually referred to as flexible chains of up to 30-50 amino acids. The ability to form peptide bonds to link amino acids together is 100 years old. Although the first peptides to be synthesized including insulin and oxytocin that did not occur for another 50-60 years.

For the last years, advances in protein synthesis and methods have developed to the point. Today peptide synthesis is a common approach in even high-throughput biological research. Advantage of peptide synthesis strategies having the capacity to form peptides that are found in biological specimens, imagination and creativity can be tapped to produce individual peptides.

Application of synthetic peptides:

The invention of peptide synthesis in the fifties spurred the development of various application areas in which synthetic peptides are now used that includes the development of epitope-specific antibodies against pathogenic proteins, the study of protein functions and the characterization and the identification of the protein. Synthetic peptides are mainly used to study enzymes substrate interaction within enzyme classes such as protease and kinases.

Synthetic peptides can resemble occurring peptides and they act as drugs against many major diseases especially for cancer. Synthetic peptides are used as reagents in the mass spectrometry-based application and it plays a central role in mass spectrometry (MS) based characterization and quantitation of proteins.

Process of synthesizing peptides:

Peptide synthesis is occurred by coupling the carboxyl group of the incoming amino acid to N-terminus of the growing peptide chain. C-to-N synthesis is opposite from protein biosynthesis and this is during which the N-terminus of the incoming amino acid is linked to the C-terminus of the protein chain. The addition of amino acids to the growing peptide chain occurs in the precise, this all due to the complex nature of in vitro protein synthesis. A common method of synthesis has a critical difference and they follow the same stepwise method to add amino acids one at a time to the growing peptide chain.

Peptide deprotection:

Amino acids have multiple reactive groups and peptide synthesis should be carefully performed to avoid side reaction. The side reaction can reduce the length and cause branching of the peptide chain. To minimize side reactions, the chemical group has been developed that bind to the amino acid reactive groups and block the functional group from the nonspecific reaction.

If the peptide synthesis is completed then all remaining protection groups are removed from the nascent peptides. There are three types of protecting groups that are used depending on the methods of peptide synthesis. Some of the contract manufacturing organization services for peptides and biopharmaceutical at clinical. From this article, you have some information about the peptide synthesis and their importance and application and also its uses.