Molecular design and biophysical studies of a new class of lipid II-binding antibiotics

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New designs of antimicrobial peptides are urgently needed in order to combat the threat of antibiotic resistance. The complex polycyclic peptide nisin is a promising lead, as it binds selectively to lipid II (only found in bacteria) and forms nisin-lipid II pores which cause lysis of the bacterial cell membrane. However, to exploit this fully it is necessary to understand how the peptide structure and sequence influence both the molecular architecture of the pore and the kinetics of pore formation. This project will have both academic impact, through developing a chemical biology approach to a better understanding of the molecular recognition of this unique pore complex (academic), and industrial and societal impact, as it will form the basis for libraries of potent, simplified candidate peptides for screening for antimicrobial activity.