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Bis‐Lactam Peptide [ i , i + 4]‐Stapling
Author(s) -
Hu Xiao,
Wu Bo,
Zheng Weiping
Publication year - 2019
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201800446
Subject(s) - lactam , helicity , chemistry , peptide , stereochemistry , biochemistry , physics , particle physics
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°C). 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 N ε ‐ para ‐phenylenediacetyl‐lysine was able to afford a % α‐helicity value of ~64.1% (25°C). Therefore, the bis‐lactam [ i , i + 4]‐stapling could also be an efficacious peptide stapling mode that can be employed for biomedical applications.