A game-changer for patients at risk of rapid health deterioration, such as heart complications, stroke, sepsis and cancer.
From: Monash University
January 25. 2021 -- The research team,
led by Dr Simon Corrie from Monash University's Department of Chemical
Engineering and the ARC Centre of Excellence in Convergent Bio-Nano Science and
Technology, took an antibody that binds EGFR (epidermal growth factor receptor)
proteins and engineered it to monitor the concentration of EGFR proteins in
serum solutions over time.
Co-authors of the paper, published
in ACS Sensors, are Dr Christian Fercher, Dr Martina Jones and
Professor Stephen Mahler from The University of Queensland and the Australian
Institute for Bioengineering and Nanotechnology.
An inability to detect the growth of
EGFR proteins in humans can be associated with the development of a number of
tumours, including cancer, as well as the onset of diseases like Alzheimer's.
Using an independent detection mechanism
developed by the research team, involving fluorescent dyes, researchers created
a biosensor from a well-known antibody that was able to 'read out' changes of
the EGFR protein in real-time by monitoring detectable changes in the
fluorescence spectra.
The ability to monitor protein biomarker
concentrations in body fluids in real-time is invaluable for tracking patients
at risk of rapid deterioration, including those requiring personalised drug
monitoring or those at high risk of complications arising from critical
conditions, like sepsis, heart attack or tumour response to treatment.
No one has been able to engineer an
antibody for continuous testing until now.
"All the diagnostic tests that we
are familiar with involve sampling something (blood, urine, tissue) at a
particular point in time and taking the same to a lab to interrogate it. But
for patients suffering from acute conditions, in which time to diagnose and
rapid treatment are very important, this traditional diagnostic process is not
good enough," Dr Corrie said.
"Monitoring dynamic changes in
proteins, for example protein levels increasing or decreasing over time, is
likely to provide much more detailed information about a disease or treatment
process, but the sensors required to do this don't exist outside of continuous
glucose testing for diabetes.
"Our capacity to create antibodies,
which bind reversibly to targets and can be 'read out' using fluorescence,
means we can develop in vivo sensors. These sensors can monitor the levels of
critical biomarkers as they change over time in response to a disease or
treatment, rather than just sending a sample to a lab and getting a snapshot in
a day or two.
"These biomarkers could include the
amount of surface proteins on a cancer cell and whether or not a drug causes
them to reduce in size, therefore testing the efficacy of treatment. It can
also be used to monitor the concentration of potentially toxic drugs, like some
antibiotics."
This discovery was able to engineer an
antibody fragment capable of reversibly binding to a protein analyte (scFv) in
a chemical solution, while retaining the specificity of the original antibody
sequence.
Through their efforts, continuous in
vitro monitoring over multiple hours was successfully recorded.
"Work is underway to employ dyes
that are much better suited to medical applications," Dr Corrie said.
"In future, we expect that this
process will be used to generate a range of biosensors that can monitor protein
concentration continuously inside the human body, through a biopharmaceutical
process, or in the environment."
https://www.sciencedaily.com/releases/2021/01/210125094323.htm
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