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Printable Handouts
Navigable Slide Index
- Introduction
- Proteomics and mass spectrometry
- LC-MS workflow
- Mass spectrometry-based proteomics
- Drug discovery pipelines
- Applications of proteomics at different stages of drug discovery
- Preclinical and clinical testing
- Target identification/deconvolution
- Strategies for drug target deconvolution
- Global PTM profiling
- Enrichment strategies for global PTM profiling
- Histone PTM profiling
- Chemical proteomics
- Quantitative chemical proteomics
- Quantitative chemical proteomics: Kd determination
- Activity-based probe profiling (ABPP)
- Drawbacks of chemical proteomics
- Ligand-induced thermal stabilization
- Cellular Thermal Shift Assay (CETSA)
- Thermal proteome profiling
- Melting curves and dose response curves
- 2D-thermal proteome profiling
- Chemical proteomics vs. TTP
- Conclusions
Topics Covered
- Mass spectrometry-based proteomics
- Applications of proteomics at different stages of drug discovery
- Target identification / deconvolution
- Post translational modification profiling (Histone profiling)
- Chemical proteomics
- Activity-based probe profiling (ABPP)
- Thermal proteome profiling
- Cellular Thermal Shift Assay (CETSA)
Talk Citation
Noberini, R. (2025, September 30). Proteomics in drug discovery [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved September 30, 2025, from https://doi.org/10.69645/ICNF7403.Export Citation (RIS)
Publication History
- Published on September 30, 2025
Financial Disclosures
- There are no commercial/financial matters to disclose.
A selection of talks on Biochemistry
Transcript
Please wait while the transcript is being prepared...
0:00
Hi, everybody. I'm Roberta
Noberini, and I work as
a staff scientist at the European
Institute of Oncology in Milan, Italy.
Welcome to this talk about how
proteomics contributes
to drug discovery.
0:17
Proteomics is the global
analysis of proteomes.
Meaning the proteins
produced by an organism,
system, or biological context
in a specific time frame.
Nowadays, the most
common tool used in
proteomics is mass
spectrometry, also called MS.
It's an analytical
technique that is
used to measure the
mass-to-charge ratios
of ions, allowing to
precisely determine
the mass of different molecules,
including peptides and
proteins, which are
the most relevant in the
context of this talk.
During this talk, when I
talk about proteomics,
I'm going to refer to
mass spectrometry-based
proteomics.
1:04
Mass spectrometry is
typically coupled with
liquid chromatography
separation,
which occurs online
prior to MS analysis
and separates the mixture
with multiple components.
A typical liquid
chromatography mass
spectrometry or LC-MS workflow
is depicted here.
First, the proteins are
extracted from the cells
or tissues of interest.
Then they are digested into
peptides by using a protease.
Trypsin, which cuts
at the levels of
arginine and lysine amino acids,
is the most commonly
used protease.
But others can be employed
for specific applications.
The peptides are separated by
liquid chromatography,
ionized, and analyzed in
the mass spectrometer,
where the mass overcharge
ratios of the peptides
and of peptide
fragments are measured.
This information is
then searched against
the sequence database to
identify peptide sequences and
from there obtain protein identifications,
post-translation and modifications
identification, together with
their localization as well
as protein quantifications.
Mass spectrometry-based
proteomics can be