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Title: Biocompatible macrocyclization between cysteine and 2-cyanopyridine generates stable peptide inhibitors
Authors: Nitsche, Christoph
Onagi, Hideki
Quek, Jun-Ping
Otting, Gottfried
Luo, Dahai
Huber, Thomas
Keywords: Science::Medicine
Issue Date: 2019
Source: Nitsche, C., Onagi, H., Quek, J.-P., Otting, G., Luo, D., & Huber, T. (2019). Biocompatible macrocyclization between cysteine and 2-cyanopyridine generates stable peptide inhibitors. Organic Letters, 21(12), 4709-4712. doi:10.1021/acs.orglett.9b01545
Journal: Organic Letters
Abstract: Peptides featuring an N-terminal cysteine residue and the unnatural amino acid 3-(2-cyano-4-pyridyl)alanine (Cpa) cyclize spontaneously in aqueous solution at neutral pH. Cpa is readily available and easily introduced into peptides using standard solid-phase peptide synthesis. The reaction is orthogonal to all proteinogenic amino acids, including cysteine residues that are not at the N-terminus. A substrate peptide of the Zika virus NS2B-NS3 protease cyclized in this way produced an inhibitor of high affinity and proteolytic stability.
ISSN: 1523-7060
DOI: 10.1021/acs.orglett.9b01545
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Organic Letters, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles

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