Dear Sir. Concerning your issue about the protocol to make long peptides using biotechnological approach. A technique that has been relatively recently developed involves attaching one end of the peptide to a solid polymer, meaning that the peptide cannot get washed away along with the excess acid. This is much quicker than classical synthesis, and leads to dramatically improved yields. The process consists of five steps carried out in a cyclic fashion. Step 1 - Attaching an amino acid to the polymer The amino acid is reacted with a molecule known as a "linkage agent" that enables it to attach to a solid polymer, and the other end of the linkage agent is reacted with the polymer support. Step 2 - Protection An amino acid is an acid with a basic group at one end and an acid group at the other. To prevent an amino acid from reacting with itself, one of these groups is reacted with something else to make it unreactive. Step 3 - Coupling The protected amino acid is then reacted with the amino acid attached to the polymer to begin building the peptide chain. Step 4 - Deprotection The protection group is now removed from the acid at the end of the chain so it can react with the next acid to be added on. The new acid is then protected (Step 2) and the cycle continues until a chain of the required length has been synthesised. Step 5 - Polymer removal Once the desired peptide has been made the bond between the first amino acid and the linkage agent is broken to give the free peptide. For more details, I think the following below link may help you in your analysis:
Fmoc solid phase peptide synthesis would be the approach used and follows the same protocol as provided by Isam. Fmoc is the protecting group for the α-amine group of the amino acids and the chemistry involved with all the protocols required for this approach are well reviewed in Fmoc solid phase peptide synthesis by Chan and White, 2000.