The production of peptides into the various amino acids and the linking to amine bonds, or peptides, are called peptide synthesis. The biological process that involves the production of peptides is called protein biosynthesis. The action of peptide synthesis enhances the study of the protein functions characterization and application of proteins and the development of epitope-specific antibodies against pathogenic proteins.

The peptide synthesis also helps study the enzyme-substrate interaction within the important enzyme classes such as proteases that play a vital role in cell signalizing and kinase and synthetic peptides used as a base application reagents MS (mass spectrometry).

The Factors You Should Know About Peptide Synthesis

As discussed, the sequence of creating peptides made up of several amino acids connected to the amide bonds is known as peptide bonds. The condensation reaction is by chemical synthesizing one amino acid’s carboxyl group to the other amino group.

There is a need to protect the group strategies to avoid undesirable reactions from many amino acid side chains. The peptide synthesis companies offer a variety of options for synthesis. The initiation of the peptides is generally at the peptides carboxyl end (C terminus) and the signs of progress of the amino terminus, also known as the N(terminus).

In a living organism, the protein biosynthesis or long peptides typically occurs in opposite directions. Peptide synthesis naturally moves in different stages. Below are the five things about the peptide synthesis process.

  1. Peptide Deprotection

Amino acids have several reactive groups. When carefully carried, the synthesis prevents the reaction and enables the shortening and branching of the peptide chain. The manufacture of the peptides with minimal responses allows the amino acid reactive groups, analysis to bind the functional group and prevent nonspecific reactions.

The individual amino acids are first reacted with the protective groups before they synthesize peptides. Shortly after coupling, the newly added amino acids are deprotected, allowing the amino acids that follow to bind correctly into the growing peptide chain. After the peptide synthesis, the protecting groups remain until the removal of the nascent peptides.

  1. Amino Acid Coupling

Carbodiimide activation is necessary for peptide synthesis coupling using the dicyclohexylcarbodiimide (DCC) or diisopropyl Carbodiimide (DIC). During the coupling of the reagent reacts, it forms a highly reactive O-acylisourea that quickly intermediates as displacement causes the nucleophilic to attack from the N-terminal primary amino group.

The reactive nature of the acrbohydarest causes amino acids to have several racemizations. At this stage, the researcher can reduce the risk of racemization by adding reagents. The reagents react with the O-acylisourea intermediate. It is less reactive and requires activating bases that direct amino acid coupling.

  1. Peptide cleavage

After the successive round of deprotection and coupling, removing all the intact protecting groups from the nascent peptide is necessary. The chemical that breaks up the acidolysis depends on the protection scheme. the strong acids, namely

  • Hydrogen bromide (HBr)
  • hydrogen fluoride (HF), or trifluoromethane sulfonic
  • cleaves Boc
  • Bzl

When cleavage conduction is appropriate, it can remove the N-terminal protection group of the last amino acids. In addition is the removal of the C-terminal protection group, which Is either a resin or chemical from the first amino acid with any of the side protective groups.

At this step, the scavengers react to free the protecting groups. Also, to avoid the acid catalyzation side reactions, the researchers usually optimize the peptide synthesis to prevent the cleavage reaction.

  1. Peptide synthesis strategies

Over the years, scientists have continued to synthesize peptides using the liquid phase peptide synthesis, which reveals that it is one of the most common methods. However, this method is slow and labor-intensive since the removal is manual. The technique involves different chemical groups that protect the C-terminus of the first amino acid with the liquid phase synthesis.

It is easier to detect product purification after every single step. In addition, it’s possible for the convergent synthesis performance due to the synthesis of the peptide sequence that links together, making a larger molecule. Rather than having chemical groups that protect the C-terminus, the first amino acid has its C-terminus coupled to the rigid activated support.

  1. Peptide Purification

Currently, it is now possible for the mass production of peptides. Numerous reactions have a free protecting group, such as incomplete deprotection causes truncation, isomers, or the deletion of sequences. At this stage, the negative effect of the peptide synthesis has a greater chance for the production of the negative impact of the synthesis that targets peptides. Therefore, the peptide yield is contrary to the peptide length.


Previously the peptide synthesis produced low yields, which is labor-intensive. However, the use of the peptides in developing new enzymes, vaccines, and drugs that include antibodies target specific epitopes. The mapping enzyme is for general research studies that involve improving and manufacturing peptide chemistry techniques.