Ultrafast 2DIR Spectroscopy for Biomedical Analysis
Lead Research Organisation:
University of Strathclyde
Department Name: Physics
Abstract
The project explores the application of ultrafast 2D-IR spectroscopy as a novel analytical tool for use in biomedical analysis. 2D-IR spectroscopy has been demonstrated to be a powerful tool for use in analysing complex spectra and for obtaining information on molecular structure, spectroscopy and dynamics of a range of biological molecules. This work has paved the way for the method to be applied in the analysis of complex biofluids such as blood plasma or serum for rapid, non-invasive disease diagnosis. However, significant technical and physical science challenges must be overcome in order to make the measurements practical and to develop the tools required for a comprehensive understanding of the spectra produced.
This project will begin by obtaining 2D-IR spectra of model blood plasma consisting of aqueous solutions of soluble, commercially-available proteins, making the mixtures more complex as the project progresses in order to establish measurement protocols and the limits of experimental sensitivity. To put the challenges into context, these will be the first measurements, on a global scale examining the amide I 2D-IR response of proteins in aqueous solution, which will offer considerable new insight into the dynamics of proteins in solution and the impact of the often-employed deuteration IR spectroscopy technique on our current understanding of their molecular physics. In parallel with this work will be development of data analysis tools based on multivariate and higher order analysis for data presentation and information retrieval.
This project will begin by obtaining 2D-IR spectra of model blood plasma consisting of aqueous solutions of soluble, commercially-available proteins, making the mixtures more complex as the project progresses in order to establish measurement protocols and the limits of experimental sensitivity. To put the challenges into context, these will be the first measurements, on a global scale examining the amide I 2D-IR response of proteins in aqueous solution, which will offer considerable new insight into the dynamics of proteins in solution and the impact of the often-employed deuteration IR spectroscopy technique on our current understanding of their molecular physics. In parallel with this work will be development of data analysis tools based on multivariate and higher order analysis for data presentation and information retrieval.
Organisations
People |
ORCID iD |
Neil Hunt (Primary Supervisor) | |
Samantha Rutherford (Student) |
Publications
Hume S
(2019)
Measuring proteins in H 2 O with 2D-IR spectroscopy
in Chemical Science
Hume S
(2020)
2D-Infrared Spectroscopy of Proteins in Water: Using the Solvent Thermal Response as an Internal Standard
in Analytical Chemistry
Studentship Projects
Project Reference | Relationship | Related To | Start | End | Student Name |
---|---|---|---|---|---|
EP/N509760/1 | 30/09/2016 | 29/09/2021 | |||
1810876 | Studentship | EP/N509760/1 | 30/09/2016 | 30/03/2020 | Samantha Rutherford |
Description | Devised a method to measure proteins in their physiological water solvents using 2D-IR without the interference of overlapping water vibrations. Then went on to measure proteins in water and blood serum (~92% water) and developed a method to directly measure the albumin to globulin ratio of serum - this is currently not directly measured in a clinical setting, total proteins and albumins are measured and what is not albumin is assumed to be globulins. Studies have shown that this ratio can help tell of a patients response to specific therapies and also of liver and kidney function, amoung other things. |
Exploitation Route | Further development |
Sectors | Healthcare Manufacturing including Industrial Biotechology Pharmaceuticals and Medical Biotechnology |