Detailed Explanation
A peptide produced by genetically engineered cells (typically E. coli bacteria, yeast, or CHO mammalian cells) rather than by chemical synthesis. The gene encoding the peptide is inserted into the host cell's DNA, and the cell's own ribosomal machinery produces the peptide during fermentation. Recombinant production is preferred for larger peptides (>50 amino acids) where SPPS yields become impractical, and for peptides requiring complex post-translational modifications that chemical synthesis cannot replicate.
Recombinant human insulin (Humulin, produced in E. coli, 1982) was the first recombinant peptide drug. Recombinant growth hormone, erythropoietin, and interferon followed. The main disadvantage is that bacterial hosts cannot perform many eukaryotic post-translational modifications.
Key Facts
- A peptide produced by genetically engineered cells (typically E. coli bacteria, yeast, or CHO mammalian cells) rather than by chemical synthesis.
- The gene encoding the peptide is inserted into the host cell's DNA, and the cell's own ribosomal machinery produces the peptide during fermentation.
- Recombinant production is preferred for larger peptides (>50 amino acids) where SPPS yields become impractical, and for peptides requiring complex post-translational modifications that chemical synthesis cannot replicate.
- Recombinant human insulin (Humulin, produced in E. coli, 1982) was the first recombinant peptide drug.
- Recombinant growth hormone, erythropoietin, and interferon followed.
- The main disadvantage is that bacterial hosts cannot perform many eukaryotic post-translational modifications.
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