F. (Fleur) Ruijne, MSc

Creating new-to-nature antimicrobial peptides via ribosomal synthesis

Nature has been the inspiration and source of many complex antimicrobials we are using in modern medicine to combat antibiotic resistance. The main focus and inspiration of research of this lab has been on the Ribosomally synthesized and posttranslationally modified peptides (RiPPs), particularly the lantibiotic nisin. As the name RiPPs implies, these complex peptides are ribosomally produced and subsequently heavily modified by specific enzymes to create new chemical moieties; for instance a lanthionine ring in the case of nisin. Over the past few years, many of these posttranslational modification enzymes have been discovered, introducing many different types of modifications. These are unexplored enzymes from sponge symbionts, other marine environments and also the gut microbiome.

Our goal is to orchestrate several of these enzymes to work on the same substrate peptide in vivo to create complex new-to-nature peptides, hereby aimed on the production of novel antimicrobials. This requires the design of a hybrid peptide that can be recognized by multiple modification enzymes. Ideally, we will design a plug-and-play system that can be combined with mutagenesis of the gene encoded peptide for facile development of novel antimicrobials.