Semi-Synthesis of Undecaprenol Analogues to Probe the Mechanism of Glycolipid-Processing Enzymes

Research output: Contribution to conferencePosterpeer-review


Polyprenols fulfil many important biological functions in bacteria, plants and animals. One such polyprenol, undecaprenol, is the universal lipid carrier in bacteria and serves to tether the lipophilic head group of glycolipids to the cytoplasmic membrane. The glycolipids lipid I and lipid II are key membrane-embedded intermediates in the synthesis of the glycopolymer peptidoglycan, which is vital to the structural integrity of bacterial cells. As such, the enzymes that process undecaprenyl-containing glycolipids, and these glycolipids themselves, represent excellent antimicrobial targets in the fight against antibacterial resistance.
The Cochrane lab have developed an optimised Soxhlet extraction procedure to obtain undecaprenol from bay leaves, which consistently yields multi-gram quantities of this valuable polyprenol. Although the lipophilic head of most bacterial glycolipids varies considerably, the undecaprenyl chain remains the same, making it an ideal site for modification. To this end, we have elaborated undecaprenol to include several chemical probes such as isotopic labels, fluorophores, and spin-labels, yielding a library of new probes for enzymatic testing. Some of these probes are currently being used in our group to study lipid II-binding antimicrobial peptides and enzymes that process undecaprenyl-containing biomolecules.
Original languageEnglish
Publication statusPublished - 20 May 2019
EventRSC Chemical Biology Symposium - Burlington House, London, United Kingdom
Duration: 20 May 201920 May 2019


ConferenceRSC Chemical Biology Symposium
Country/TerritoryUnited Kingdom


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