Overall Shape Constraint of Alternating α/β-Hybrid Peptides Containing Bicyclic β‑Proline

Our NMR, IR/Raman, CD spectroscopic, and X-ray crystallographic studies, as well as accelerated molecular dynamics simulations, showed that alternating hybrid α/β-peptides containing a bicyclic β-proline surrogate form unique extended curved folds, regardless of the peptide length and solvent enviro...

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Bibliographic Details
Published in:Organic letters 2019-10, Vol.21 (19), p.7813-7817
Main Authors: Wang, Siyuan, Otani, Yuko, Zhai, Luhan, Su, Aoze, Nara, Masayuki, Kawahata, Masatoshi, Yamaguchi, Kentaro, Sada, Akane, Ohki, Rieko, Ohwada, Tomohiko
Format: Article
Language:English
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Summary:Our NMR, IR/Raman, CD spectroscopic, and X-ray crystallographic studies, as well as accelerated molecular dynamics simulations, showed that alternating hybrid α/β-peptides containing a bicyclic β-proline surrogate form unique extended curved folds, regardless of the peptide length and solvent environment. It is suggested that extended β/PPII structures are preferred in the insulating α-alanine moieties between the rigid bicyclic β-proline structures. These hybrid peptides inhibit p53-MDM2 and p53-MDMX protein–protein interactions.
ISSN:1523-7060
1523-7052
DOI:10.1021/acs.orglett.9b02799