ORCID Profile
0000-0001-8006-8395
Current Organisation
University Of Strathclyde
Does something not look right? The information on this page has been harvested from data sources that may not be up to date. We continue to work with information providers to improve coverage and quality. To report an issue, use the Feedback Form.
Publisher: SAGE Publications
Date: 23-09-2021
DOI: 10.1177/00037028211021846
Abstract: This Focal Point Review paper discusses the developments of biomedical Raman and infrared spectroscopy, and the recent strive towards these technologies being regarded as reliable clinical tools. The promise of vibrational spectroscopy in the field of biomedical science, alongside the development of computational methods for spectral analysis, has driven a plethora of proof-of-concept studies which convey the potential of various spectroscopic approaches. Here we report a brief review of the literature published over the past few decades, with a focus on the current technical, clinical, and economic barriers to translation, namely the limitations of many of the early studies, and the lack of understanding of clinical pathways, health technology assessments, regulatory approval, clinical feasibility, and funding applications. The field of biomedical vibrational spectroscopy must acknowledge and overcome these hurdles in order to achieve clinical efficacy. Current prospects have been overviewed with comment on the advised future direction of spectroscopic technologies, with the aspiration that many of these innovative approaches can ultimately reach the frontier of medical diagnostics and many clinical applications.
Publisher: Royal Society of Chemistry (RSC)
Date: 2022
DOI: 10.1039/D2AN00978A
Abstract: Two-Dimensional Infrared (2D-IR) spectroscopy is used to detect binding of paracetamol with proteins in blood serum. Quantitative peak patterns are observed indicating structural changes of the albumins' secondary structure when paracetamol bound.
Publisher: American Chemical Society (ACS)
Date: 27-01-2020
Publisher: Royal Society of Chemistry (RSC)
Date: 2020
DOI: 10.1039/C9AN02035G
Abstract: Recent progress in laser technology and data analysis methods has enabled high throughput applications of ultrafast two-dimensional infrared (2D-IR) spectroscopy measurements and opened the door to analytical applications.
Publisher: AIP Publishing
Date: 22-11-2022
DOI: 10.1063/5.0127680
Abstract: The ability of two-dimensional infrared (2D-IR) spectroscopy to measure the amide I band of proteins in H2O rather than D2O-based solvents by evading the interfering water signals has enabled in vivo studies of proteins under physiological conditions and in biofluids. Future exploitation of 2D-IR in analytical settings, from diagnostics to protein screening, will, however, require comparisons between multiple datasets, necessitating control of data collection protocols to minimize measurement-to-measurement inconsistencies. Inspired by analytical spectroscopy applications in other disciplines, we describe a workflow for pre-processing 2D-IR data that aims to simplify spectral cross-comparisons. Our approach exploits the thermal water signal that is collected simultaneously with, but is temporally separated from the amide I response to guide custom baseline correction and spectral normalization strategies before combining them with Principal Component noise reduction tools. Case studies show that application of elements of the pre-processing workflow to previously published data enables improvements in quantification accuracy and detection limits. We subsequently apply the complete workflow in a new pilot study, testing the ability of a prototype library of 2D-IR spectra to quantify the four major protein constituents of blood serum in a single, label-free measurement. These advances show progress toward the robust data handling strategies that will be necessary for future applications of 2D-IR to pharmaceutical or biomedical problems.
Publisher: American Chemical Society (ACS)
Date: 09-12-2020
Publisher: Royal Society of Chemistry (RSC)
Date: 2019
DOI: 10.1039/C9SC01590F
Abstract: 2D-IR spectroscopy is used to measure protein amide I bands in water, avoiding the need for deuteration. We show that H/D exchange affects protein vibrational relaxation dynamics and that the ability to perform 2D-IR in water enables blood serum protein analysis.
Publisher: AIP Publishing
Date: 17-01-2023
DOI: 10.1063/5.0129480
Abstract: The form of the amide I infrared absorption band provides a sensitive probe of the secondary structure and dynamics of proteins in the solution phase. However, the frequency coincidence of the amide I band with the bending vibrational mode of H2O has necessitated the widespread use of deuterated solvents. Recently, it has been demonstrated that ultrafast 2D-IR spectroscopy allows the detection of the protein amide I band in H2O-based fluids, meaning that IR methods can now be applied to study proteins in physiologically relevant solvents. In this perspective, we describe the basis of the 2D-IR method for observing the protein amide I band in H2O and show how this development has the potential to impact areas ranging from our fundamental appreciation of protein structural dynamics to new applications for 2D-IR spectroscopy in the analytical and biomedical sciences. In addition, we discuss how the spectral response of water, rather than being a hindrance, now provides a basis for new approaches to data pre-processing, standardization of 2D-IR data collection, and signal quantification. Ultimately, we visualize a direction of travel toward the creation of 2D-IR spectral libraries that can be linked to advanced computational methods for use in high-throughput protein screening and disease diagnosis.
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Samantha Rutherford.