摘要
Summary of main observation and conclusion Even though the bis‐lactam peptide stapling with the [i, i + 7] and the [i, i + 11] systems has been known to be able to afford %α‐helicity values up to 100%(25°C), the performance of the bis‐lactam peptide stapling with the [i, i + 4] system in current literature has been mediocre (%α‐helicity ≦40%, 25℃). In the current study, we found that high %α‐helicity is also obtainable with the bis‐lactam [i, i + 4]‐stapling by demonstrating with our model peptide sequence that the bis‐lactam [i, i + 4]‐stapling with Nε‐para‐phenylenediacetyl‐lysine was able to afford a %α‐helicity value of ~64.1%(25℃). Therefore, the bis‐lactam [i, i + 4]‐stapling could also be an efficacious peptide stapling mode that can be employed for biomedical applications.
