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What is Peptide Synthesis?
Characterized by the formation of a peptide bond between two amino acids, peptide synthesis is, essentially, the production of peptides. Though peptide synthesis was somewhat hampered by relatively inefficient production practices at its inception, advancements in chemistry and technology have led to vastly improved synthesis methods. With the strong growth of the field of peptide science, it is clear that synthetic peptides will continue to play vital roles in areas of scientific and medical progress in the modern age.
How Peptides are Synthesized?
Peptides are synthesized by linking two amino acids together. This is most often accomplished by attaching the C-terminus, or carboxyl group, of one amino acid to the N-terminus, or amino group, of another. Unlike protein biosynthesis, which involves N-terminus to C-terminus linkage, peptide synthesis occurs in this C-to-N fashion.
While there are twenty amino acids that occur commonly in the natural world (such as arginine, lysine, and glutamine), many other amino acids have also been synthesized. This allows for abundant possibilities in the creation of new peptides. However, amino acids have numerous reactive groups that can negatively interact during the synthesis process, leading to unwanted truncating or branching of the peptide chain or causing suboptimal purity or yield. As a result, peptide synthesis is a complex process that must be expertly carried out.
In order to ensure the desired outcome from the synthesis process and avoid extraneous, unwelcome reactions, certain amino acid reactive groups must be deactivated, or protected, from reacting. Thus, scientists have engineered special chemical groups designed to do just that. Called “protecting groups,” they can be separated into three categories:
N-terminal protecting groups – These groups protect the N-termini of amino acids. Referred to as temporary protecting groups, they are removed relatively easily to facilitate the formation of peptide bonds. Tert-butoxycarbonyl (Boc) and 9-fluorenylmethoxycarbonyl (Fmoc) are two frequently used N-terminal protecting groups.
C-terminal protecting groups – These groups protect the C-terminus of amino acids. The use of C-terminal protecting groups is warranted in liquid-phase peptide synthesis but not solid-phase peptide synthesis.
Side chain protecting groups – As amino acid side chains are quite conducive to reactivity during peptide synthesis, various unique side chain protecting groups are needed to protect against unwanted reactions. Able to remain intact during the many cycles of chemical treatment during synthesis, side chain protecting groups are known as permanent protecting groups. They are only removed with strong acids after the conclusion of peptide synthesis.
