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Microcin J25 Antimicrobial Peptide

Images courtsey Andrew Ferguson

Microcin J25 is a small 21-residue antimicrobial peptide exhibiting an interesting "lasso" motif whereby the N-terminal glycine 1 is covalently bonded via a peptide bond to the glutamic acid 8 sidechain to form a loop through which the C-terminus is threaded and sterically locked in place by bulky aromatic groups either side of the ring. This motif imparts great thermal and chemical stability, with the peptide remaining active after exposure to boiling water and high denaturant concentrations. A current experimental and theoretical collaboration between the Link and Panagiotopoulos groups is attempting to understand the formation of this structure and replicate it in vitro by "click" chemistry inspired incorporation of non-canonical amino acids into the native peptide. 

For more infomation about Professor Debenedetti's research please see the Debenedetti Research Group site.

For more infomation about Professor Link's research please see The Link Lab site.

For more infomation about Professor Panagiotopoulos's research please see the Panagiotopoulos Research Group site.