Consecutive Cyclic Pentapeptide Modules Form Short α‐Helices that are Very Stable to Water and Denaturants | Zendy

Shepherd Nicholas E. | Zendy; Abbenante Giovanni | Zendy; Fairlie David P. | Zendy

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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).

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