Autor: |
Nemati, Mohammadmahdi, Ahmadi, Ahmadreza, Hashemzehi, Ahmad, Nasrullozoda, Farukhruzi, Abedi, Mohsen, Hashemzaei, Masoud |
Zdroj: |
International Journal of Peptide Research & Therapeutics; Jan2024, Vol. 30 Issue 1, p1-8, 8p |
Abstrakt: |
Peptides as drugs are a promising therapeutic method. Peptides modulate diverse biological processes and are synthesized with high purity. Due to their low cell permeability, peptide drugs target extracellular receptors. The peptibody comprises the biologically active Fc region and the peptide itself. Various peptides with specific biological activities have been successfully fused into the Fc region. These peptide-Fc fusions, also known as peptibodies, offer an excellent therapeutic alternative to monoclonal antibodies. They comprise biologically active peptides bound to the Fc region. This approach retains antibodies' beneficial characteristics, especially the enhanced affinity resulting from Fc dimerization and extended plasma residence time. Peptibodies can be produced in Escherichia coli using recombinant methods. In this study, we describe peptibodies and analyze different types of peptibodies collected for research. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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