Research progress in the development of long-acting technologies for protein and peptide drugs (Part 1)

Since Robert Bruce Merrifield synthesized the first biologically active peptide in 1953, research on peptide drugs has developed rapidly, and research on peptide drugs targeting multiple receptors has even been carried out internationally

To improve the stability of protein and peptide drugs, prolong the half-life in the body, and make it long-acting

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Some metabolically unstable amino acids contained in protein and peptide drugs will greatly affect the half-life of the drug.

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Linear peptides are therapeutically limited by factors such as metabolism and poor conformational stability, which may damage their biological activity and affect half-life.

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Chemical modification is a long-acting technology commonly used in protein and peptide drugs.

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The gene fusion expression of the fusion protein and the protein polypeptide drug can increase the relative molecular weight of the drug, reduce the renal clearance rate in the body, and achieve the purpose of prolonging the half-life of the drug in the body

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Glycosylation usually occurs in macromolecules such as nucleic acids, proteins, and lipids, and plays an important role in biological processes such as inflammation, immune response, and intracellular transport

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Stapling peptide is a new structural peptide in recent years, which has attracted the attention of researchers because of its very stable structure

references:

[1] Liu Meng, Yu Pengcheng, Xu Hanmei.

[2] Ding Yuan, Chen Xin, Tu Jiasheng, Sun Chunmeng.
Research progress in long-acting formulation technology of protein and peptide drugs[J].
Journal of China Pharmaceutical University, 2020, 51(04):433-440.

[3] Pang Liran, He Cheng, Wei Jingshuang, Gao Jian.
Research strategy for long-acting technology of protein and peptide drugs[J].
Advances in Biotechnology, 2021, 11(03): 304-310.