School of Physical and Chemical Sciences

 

Project Number: 2019-30

Project Leader: Richard Hartshorn, Daniel Holland

Host Department: Chemistry

Project Title: Quantification of the stability of a urease inhibitor

Project outline: Urease inhibitors are used on urea fertiliser to slow the conversion of urea to ammonium until sufficient rain or irrigation is able to wash the urea into the soil Urease inhibitors are typically applied to the surface of the urea granules during manufacturing. The coated urea is handled many times prior to application to the field. The purpose of this project is to investigate the stability of the urease inhibitor through the manufacturing process and dispatch systems.

Specific Requirements: none specified

 

 

Project Number: 2019-31

Project Leader: Richard Hartshorn, Daniel Holland

Host Department: Chemistry

Project Title: Understanding the formation of odours during superphosphate manufacture

Project outline: Superphosphate is one of the key nutrients used to support the agricultural sector in New Zealand. It is manufactured here in Christchurch at Ravensdown's Hornby works site. The process mostly operates smoothly, but periodically strong odours are produced from the plant. The odours are not toxic, but they are unpleasant. The plant is located in a residential area so these odours must be eliminated prior to the emission from the stack. This project will seek to characterise the origin of the odours from the superphosphate process and hence help develop tools to mitigate the odours prior to release.

Specific Requirements: none specified

 

 

Project Number: 2019-56

Project Leader: Deborah Crittenden, Dan Foley

Host Department: School of Physical and Chemical Sciences

Project Title: Designing new drugs that break down in sunlight to avoid environmental contamination

Project outline: Traditionally, drugs have been designed for maximum chemical stability to prolong shelf life and ensure known dosages are delivered. However, this has lead to the persistence of these compounds in the environment, exerting biological effects on aquatic organisms. We propose to develop new analogues of existing drugs designed to break down under UV radiation that does not penetrate far through the skin, focussing on drugs that are known to localise to internal organs and not reach skin capillaries. We anticipate that this project will have a number of beneficial outcomes: new drug molecules that can potentially be commercialised, reduced environmental impact of those molecules, new synthetic methodologies for light-sensitive reactions and products, new knowledge about the types of functional groups that best confer photo degradability without compromising biological activity. Ultimately, the overall aim of this project is to improve human health outcomes through access to affordable medications while minimising environmental impacts.

Specific Requirements: The student must be a chemistry or biochemistry major, and have achieved good grades in organic chemistry (including at least CHEM242). Applications from second and third year students will be considered.

 

 

Project Number: 2019-134

Project Leader: Dr Daniel Foley

Host Department: School of Physical and Chemical Sciences

Project Title: Sustainable Asymmetric Synthesis of Biomedicinally-important Amino Acids

Project outline: This project will harness synthetic organic chemistry to enable the asymmetric synthesis of artificial amino acids. Amino acids are extremely important chemicals in biology, being the monomers that make up the biological macromolecules proteins, which perform nearly all the important functions of cells. Artificial amino acids have significant value in Chemical Biology, where they can be incorporated into proteins to, for instance, tag them with fluorescent labels that can be tracked in living cells, or tag them with chemical handles that allow manipulation of the protein in vivo. Interrogation of the roles of proteins in living cells is paramount to understanding the molecular mechanisms underlying disease, and towards the development of new therapeutics. While the 20 naturally-occurring proteinogenic L-amino acids are readily accessible by commercial fermentation, the enantiomeric D-amino acids, along with enantiopure artificial amino acids, are not readily accessible by currently available synthetic routes. Currently routes to artificial amino acids lack generality, or suffer from the use of toxic reagents such as cyanide. In stark contrast, this project will develop a general, environmentally-benign, one-step procedure to give access to both naturally-occurring and artificial amino acids.

Specific Requirements: The student must be a chemistry major and will have achieved good grades in organic chemistry (including at least the CHEM242 course). Applications from both second and third year students will be considered.

 

 

Project Number: 2019-135

Project Leader: Dr Jodie Johnston

Host Department: School of Physical and Chemical Sciences

Project Title: Targeting Chorismate Utilising Enzymes from the Human Pathogens that Cause Tuberculosis and MRSA

Project outline: Bacteria, including pathogens such as M. tuberculosis (M.tb, the causative agent of tuberculosis) and S. aureus (S.au, the cause of many debilitating skin and medical device infections, including hard to treat MRSA infections) rely on the correct functioning of key enzymes in their metabolic pathways to survive. Chorismate utilising enzymes convert the small molecule chorismate into a range of different products important for bacterial survival and virulence. They often act as metabolic hubs providing precursors chemicals for more than one downstream biochemical pathway. In M.tb the essential chorismate utilising enzyme EntC, converts chorismate into a precursor product that is used by two downstream pathways; one making iron-chelating siderophores vital for iron acquisition, the other making menaquinone (vitamin K) which is vital for bacterial energy generation and mediating pathogen virulence and persistence. In S.au the role of producing the precursor for making menaquinone depends on a dedicated chorismate utilising enzyme, MenF. Our laboratory has an interest in both CUEs and the enzymes that use their products to produce menaquinone. We want to understand the structure and function of these proteins in different pathogens to assist our small molecule inhibitor discovery efforts with the long-term goal of finding new antimicrobial agents. In this studentship we propose to characterise the M.tb EntC and S.au MenF and compare their functions and interactions with other enzymes in the menaquinone biosynthesis pathway. This will give help us understand why MenF serves only one pathway while EntC acts as a metabolic hub serving multiple pathways. During this project the student could expect to learn core skills in molecular biology and protein expression as well as basic biochemistry skills such as enzyme activity assays, small molecule ligand binding assays and experiments to detect protein-protein interaction.

Specific Requirements: No specific prerequisites. This project would suit a curious student motivated and interested by both biology and chemistry with an academic background in a biochemistry or chemical biology area. A passion for wanting to understand how biology works at the molecular level is a must. The willingness to learn, ask questions and work cooperatively in a research team are other very important skills required for this project.