N-methylation of peptide bonds dramatically improves oral bioavailability, proteolytic stability, and membrane permeability of peptides — the chemical modification strategy behind several successful oral peptide drugs including cyclosporine.
Key findingN-methylation of peptide backbone amides improves oral bioavailability, proteolytic stability, membrane permeability, and conformational rigidity — th
What the researchers found
N-methylation of peptide backbone amides improves oral bioavailability, proteolytic stability, membrane permeability, and conformational rigidity — the key chemical modification enabling oral peptide drugs, validated by cyclosporine and being applied to new therapeutic peptides.
Why it matters
Relevant for peptide-design, bioavailability, cyclic-peptides.
How the study worked
review study.
What this study cannot tell us
See abstract.
How to read the evidence
moderate evidence.
When this study was published
Published in 2008.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
- Clinical translation to evaluate.
Common questions
What was studied?
What was found?
Read the original research
N-methylation of peptides: a new perspective in medicinal chemistry.
Accounts of chemical research, 41(10), 1331-42
Citation
Chatterjee, Jayanta; Gilon, Chaim; Hoffman, Amnon; Kessler, Horst. (2008). N-methylation of peptides: a new perspective in medicinal chemistry.. Accounts of chemical research, 41(10), 1331-42. https://doi.org/10.1021/ar8000603