New Cyclic Peptides via Ring-Closing Metathesis Reactions and Their Anti-Bacterial Activities

T. P. Boyle, University of Wollongong
J. B. Bremner, University of Wollongong
J. Coates, Avexa
J. Deadman, Avexa
P. A. Keller, University of Wollongong
Stephen G. Pyne, University of Wollongong
D. I. Rhodes, Avexa

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This article was originally published as Boyle, TP, Bremner, JB, Coates, J, Deadman, J, Keller, PA, Pyne, SG & Rhodes, DI, New Cyclic Peptides via Ring-Closing Metathesis Reactions and Their Anti-Bacterial Activities, Tetrahedron, 64(49), 2008, 11270-11290. Original journal article available here

Abstract

As part of a program investigating cyclic peptides with an internal aromatic hydrophobic scaffold as potential novel anti-bacterial agents, we explored the synthesis of simple tyrosine-based systems. These were prepared via key intermediates containing internal allylglycine and allyltyrosine residues for subsequent ring closing metathesis reactions. Although the resulting anti-bacterial activity against Staphylococcus aureus was modest, this represents a novel and simple route to this class of compounds. One intermediate acyclic dipeptide precursor showed good activity against S. aureus with an MIC of 7.8 µg/mL.