20. Mass Spectrometry 1
Introduction to Mass Spectrometry
Lecture presented by Ben Collins from Queen’s University Belfast.
Course: BIO2102 – Experimental Biochemistry
Learning Outcomes
Students should be able to:
Explain the basics of mass spectrometry.
Describe the fundamental approaches to peptide/protein analysis by mass spectrometry.
Mass Spectrometry Outline for BIO2102
Lecture Schedule
Lecture 1: Mass spectrometry basics.
Lecture 2: Fundamentals of protein and peptide analysis by mass spectrometry.
Today's Lecture Outline
Background and basic principles.
Ionization techniques:
Focus on MALDI (Matrix-Assisted Laser Desorption/Ionization)
Focus on Electrospray Ionization.
Mass analysis techniques:
Focus on Quadrupoles.
Focus on Time-of-Flight (TOF).
Detection techniques:
Mass spectra concepts, charge states, and isotope distribution.
Overview of Tandem mass spectrometry.
History of Mass Spectrometry
Early 1900s: Development of mass spectrometry instrumentation.
Initial studies involved anode/cathode rays and isotopes.
Late 1950s: Mass spectrometry for organic chemistry:
Focus on small organic molecules (< 500 Da).
Mid 1980s: Expansion to biological mass spectrometry:
Methods for large, non-volatile biomolecules (e.g., peptides, proteins).
Influential ionization methods include Fast Atom Bombardment (FAB) and Thermospray (TSI).
Newer techniques: Electrospray Ionization (ESI), MALDI.
Proteomics revolution (early 1990s):
Significant advancements in electronics, automation, informatics, and data acquisition methods.
Nobel Prizes in Mass Spectrometry
Key Nobel Laureates:
Joseph John Thomson (1906): For investigations on conduction of electricity by gases.
Francis William Aston (1922): For discovery of isotopes and mass spectrum.
Wolfgang Paul (1989): For development of the ion trap technique.
John Bennet Fenn & Koichi Tanaka (2002): For development of ESI and MALDI methods for biological macromolecules.
General Applications of Mass Spectrometry
Pharmaceutical Applications
Bioavailability and drug metabolism studies.
Characterization of drugs and degradation products.
Screening and identifying drug targets.
Biomolecule Applications
Analysis of proteins, peptides, and oligonucleotides.
Environmental Analysis
Tracking organic pollutants and soil contamination.
Forensic Applications
Linking suspects to crimes and detecting narcotics.
Sports anti-doping analysis.
Security Applications
Detection of explosives and chemical warfare agents.
Food & Beverage Analysis
Detection of natural compounds and adulterants.
Principle of Mass Spectrometry
Ionization: Convert sample components into charged ions.
Gas Phase Transition: Volatilize the sample components.
Ion Manipulation: Use electric or magnetic fields to separate ions based on mass/charge ratio (m/z).
Detection: Count and register separated ions.
Mass Spectrometer Components
Source: Ionization techniques (e.g., ESI, MALDI).
Analyzer: Various types (Quadrupole, TOF, etc.).
Detector: Converting ions to electrons (e.g., MCP, charge induction).
Biological Mass Spectrometry Revolution (1990s)
Enabled analysis of large biomolecules with soft ionization techniques.
MALDI and Electrospray Ionization for proteins and peptides.
Ionization Methods
Electrospray Ionization (ESI)
Produces ions from liquid solutions via a strong electric field.
Operates predominantly in positive mode for peptides.
Matrix-Assisted Laser Desorption/Ionization (MALDI)
Vaporizes non-volatile samples from solid to gas state.
Mass Analysis Techniques
Time-of-Flight (TOF)
Dependent on ion size: larger ions travel slower, taking longer to traverse the drift zone.
Kinetic energy distribution defined by charge and voltage.
Quadrupole Mass Analyzer
Functions as a filter, analyzer, or trap.
Operates based on frequency of electrical switching.
Detection in Mass Spectrometry
Converts ion signals to electrical signals for detection.
Common detection methods: Impact (MCP), inductive detection.
Summary of Mass Spectrometry Basics
Involves three key stages: ionization, analysis, and detection.
Different technologies correspond to each stage and can be combined.
Next lecture will detail approaches for peptide and protein analysis.