About the Project
Cationic AMPs interact with negatively charged microbial cell membranes through electrostatic interactions. Their primary structures contain a relatively high proportion of cationic and hydrophobic amino acids, which can make them intrinsically vulnerable to protease degradation. Therefore, proteolytic instability of AMPs is a serious barrier for their effective translation into the clinic. This project aims to investigate different mechanisms for increasing the resistance of cationic AMPs to protease digestion.
Cationic AMPs engineered to withstand protease degradation will be produced, purified and characterized biochemically. The antimicrobial properties of these AMPs will be investigated against a collection of bacterial and fungal pathogens, including Mycobacterium tuberculosis and Aspergillus fumigatus. These protease-resistant AMPs will offer a novel platform for the development of a new class of antimicrobial agents with improved efficacy and resistance to degradation.
Training/techniques to be provided:
Peptide design; protein engineering; recombinant protein expression and purification; biochemical characterisation; circular dichroism spectroscopy; bacterial cultures, cell culture, antimicrobial assays to determine minimum inhibitory and minimal bactericidal concentrations.
Candidates are expected to hold (or be about to obtain) a first class or upper second class honours degree (or equivalent) in biochemistry, biology, or microbiology. Candidates with experience in Microbiology or with an interest in Infectious Diseases and Antimicrobial Resistance are encouraged to apply.
For international students we also offer a unique 4 year PhD programme that gives you the opportunity to undertake an accredited Teaching Certificate whilst carrying out an independent research project across a range of biological, medical and health sciences. For more information please visit http://www.internationalphd.manchester.ac.uk
As an equal opportunities institution we welcome applicants from all sections of the community regardless of gender, ethnicity, disability, sexual orientation and transgender status. All appointments are made on merit.
Vickers CF, Silva A, Chakraborty A, Fernandez P, Kurepina N, Saville C, Naranjo Y, Pons M, Schnettger LS, Gutierrez MG, Park S, Kreiswith BN, Perlin DS, Thomas EJ, Cavet JS, Tabernero L. Structure-based design of MptpB inhibitors that reduce multi-drug-resistant Mycobacterium tuberculosis survival and infection burden in vivo (2018). J Med Chem, 61(18): 8337-8352. doi: 10.1021/acs.jmedchem.8b00832
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