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Consecutive Cyclic Pentapeptide Modules Form Short α‐Helices that are Very Stable to Water and Denaturants
Author(s) -
Shepherd Nicholas E.,
Abbenante Giovanni,
Fairlie David P.
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200352659
Subject(s) - pentapeptide repeat , guanidine , chemistry , helix (gastropod) , trypsin , cyclic peptide , stereochemistry , peptide , crystallography , biochemistry , biology , ecology , enzyme , snail
A generic approach to mimicking α‐helices has been achieved by using sequences of consecutive macrocyclic pentapeptides (for example, cyclo(1→5)‐Ac‐[KARAD] n ‐NH 2 ) to form 3‐turn (see picture) and 4‐turn α‐helices, which have high conformational stability in water and are resistant to protein‐denaturing conditions (65 °C, 8 M guanidine⋅HCl, trypsin digestion).