An N-ortho-nitrobenzylated benzanilide amino acid enables control of the conformation and membrane permeability of cyclic peptides

Yuko Otani; Asami Ichinose; Xihong Wang; Zhihan Huang; Akitomo Kasahara; Mayumi Ishii; Eri Watanabe; Kayoko Kanamitsu; Kempei Tai; Hiroyuki Kusuhara; Takumi Ueda; Koh Takeuchi; Tomohiko Ohwada

doi:10.1039/D4CC02738H

An N-ortho-nitrobenzylated benzanilide amino acid enables control of the conformation and membrane permeability of cyclic peptides†‡

Yuko Otani,

*^a Asami Ichinose,^a Xihong Wang,^a Zhihan Huang,^a Akitomo Kasahara,^a Mayumi Ishii,^a Eri Watanabe,^a Kayoko Kanamitsu,^a Kempei Tai,^a Hiroyuki Kusuhara,^a Takumi Ueda,

*^ab Koh Takeuchi

^a and Tomohiko Ohwada

*^a

Author affiliations

* Corresponding authors

^a Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan
E-mail: otani@mol.f.u-tokyo.ac.jp, ueda@phs.osaka-u.ac.jp, ohwada@mol.f.u-tokyo.ac.jp

^b Graduate School of Pharmaceutical Sciences, Osaka University, 1-6, Yamadaoka, Suita-Shi, Osaka, Japan

Abstract

We designed and synthesized an N-ortho-nitrobenzylated benzanilide-based amino acid having a cis-amide structure that facilitates cyclization of peptides containing it. Photo-induced removal of the nitrobenzyl group from this residue in the resulting cyclized peptides dramatically alters their conformation and passive membrane permeability via complete cis-amide to trans-amide conversion.

Chemical Communications

An N-ortho-nitrobenzylated benzanilide amino acid enables control of the conformation and membrane permeability of cyclic peptides†‡

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An N-ortho-nitrobenzylated benzanilide amino acid enables control of the conformation and membrane permeability of cyclic peptides

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