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Structural Features and Binding Modes of Thioether-Cyclized Peptide Ligands

Department of Chemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, 113-0033 Tokyo, Bunkyo-ku, Japan
JST CREST, The University of Tokyo, 7-3-1 Hongo, 113-0033 Tokyo, Bunkyo-ku, Japan
Author to whom correspondence should be addressed.
Biomedicines 2018, 6(4), 116;
Received: 12 November 2018 / Revised: 10 December 2018 / Accepted: 11 December 2018 / Published: 13 December 2018
(This article belongs to the Special Issue Discovery and Development of Constrained Peptide Ligands)
PDF [3367 KB, uploaded 13 December 2018]


Macrocyclic peptides are an emerging class of bioactive compounds for therapeutic use. In part, this is because they are capable of high potency and excellent target affinity and selectivity. Over the last decade, several biochemical techniques have been developed for the identification of bioactive macrocyclic peptides, allowing for the rapid isolation of high affinity ligands to a target of interest. A common feature of these techniques is a general reliance on thioether formation to effect macrocyclization. Increasingly, the compounds identified using these approaches have been subjected to x-ray crystallographic analysis bound to their respective targets, providing detailed structural information about their conformation and mechanism of target binding. The present review provides an overview of the target bound thioether-closed macrocyclic peptide structures that have been obtained to date. View Full-Text
Keywords: macrocyclic; peptide; crystallography macrocyclic; peptide; crystallography

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Otero-Ramirez, M.E.; Passioura, T.; Suga, H. Structural Features and Binding Modes of Thioether-Cyclized Peptide Ligands. Biomedicines 2018, 6, 116.

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