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With the development of biotechnology, peptides have become more and more useful in the field of biomedicine. Protected amino acids are the most basic raw materials for solid-phase synthesis of peptides. Amino acids all contain α-amino and carboxyl groups. Some of the 20 amino acids also contain side-chain active groups, such as hydroxyl, amino, guanidine and heterocyclic groups. Different amino acids need their own protecting groups, and with the different types of synthetic peptides, the selected protecting group schemes are also different. Both the amino group and the side chain active group need to be protected in the peptide reaction. After the peptide is synthesized, the protective group is removed, otherwise the misconnection of amino acids and many side reactions will occur.
Protected amino acids are generally divided into single-protected amino acids and double-protected amino acids. Single-protected amino acids refer to protected amino acids that only protect α-amino groups; double-protected amino acids refer to amino acids that require protection of side chain active groups in addition to α-amino groups.
It can be divided into three main categories: alkoxycarbonyl, acyl and alkyl. Among them, Fooc protection in alkoxy groups is more common. Under weak alkaline conditions such as sodium carbonate or sodium bicarbonate, Fmoc-Cl or Fmoc-OSu is generally used to introduce Fmoc protecting groups. Compared with Fmoc-Cl, Fmoc-OSu is easier to control the reaction conditions and has fewer side reactions. Under acidic conditions, the Fmoc protecting group is particularly stable, but it is very sensitive to alkaline conditions, so it is usually used together with the acid-sensitive protecting group Boc or Z to protect amino acids containing active side chain groups.
The active side chains of amino acids mainly include: hydroxyl, thiol, carboxyl, amino, sarcosyl, imidazole, amide, indole and thioether groups. When synthesizing peptides, these active groups are generally protected first, and then the peptide reaction is carried out to avoid some side reactions. For example, side chain amino groups must be protected during peptide synthesis, such as lysine. Different from the α-amino protecting group, the side chain amino protecting group must be selective, and it will not be affected when the other protecting groups are removed, and then removed after the peptide is synthesized. The earliest protecting group is p-toluenesulfonyl (Tos), which has good stability and can only be removed by Na/liquid ammonia treatment. Lysine first forms a ketone complex, and then reacts with Tos-Cl under weakly alkaline conditions to selectively protect the side chain amino group and then remove copper. Using Lys (Tos), people have successfully synthesized peptides and proteins such as oxytocin, vasopressin and insulin.
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