The Boc/Bzl (tert-butoxycarbonyl/ /benzyl) method is a classical peptide solid phase synthesis method
in which Boc is used as a temporary protecting group in combination with a benzylic semi-permanent side chain protecting group.
Boc is unstable to acid and is usually removed with 20% to 50% TFA.
The main strategy of the oc synthesis method is that the Boc which can be removed by TFA is an α-amino protecting group, and the side chain is protected by a benzyl alcohol. A Boc-amino acid derivative is covalently cross-linked to a Merrifield or M BH A resin during synthesis, Boc is removed by TFA, the free amino terminus is neutralized with triethylamine, and then the next amino acid is activated by DCC. Finally, the HF method or the TFM SA method is used for the deprotection.
Although the Boc method is gradually replaced by the Fm oc method, since the Boc-amino acid is easily crystallized, it is easy to be acid-decomposed, has stability, and is easy to store for a long time. It is not easy to produce side reactions during acid hydrolysis, and is stable to alkali hydrolysis and hydrolytic hydrolysis. The advantages of stable catalytic hydrogenation can not be ignored, and some aspects are worth learning and application.
Merrifleld et al. successfully synthesized bradykinin using Boc as a protective group for α-amino acids. Australian scientist M iranda et al. rapidly synthesized peptides and small proteins including the C-terminal fragment of H IV-1 protease (81-99) and the 88-residue protein CP10 in the "chemical selective ligation" method.