Methoden vergleichen

	MALDI-TOF	Oberflächenplasmonenresonanz
Fachgebiet	Spektroskopie	Spektroskopie
Familie	Process / pipeline	Process / pipeline
Entstehungsjahr	1988	1971
Urheber	Michael Karas	Erich Kretschmann
Typ	Ionization and mass analysis technique	Optical technique
Wegweisende Quelle	Karas, M., & Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Analytical Chemistry, 60(20), 2299-2301.	Kretschmann, E. (1971). Determination of optical constants of metals by excitation of surface plasmons. Zeitschrift für Physik, 241(4), 313-324.
Aliasnamen	MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry	SPR, surface plasmon, SPR biosensing
Verwandt	3	3
Zusammenfassung	Matrix-Assisted Laser Desorption/Ionization (MALDI) combined with Time-of-Flight (TOF) mass analysis, or MALDI-TOF, is a soft ionization mass spectrometry technique that gently ionizes intact biomolecules and volatile organic compounds, then measures their mass-to-charge ratio by measuring flight time through a field-free drift region. Introduced independently by Karas, Hillenkamp, and Tanaka in 1988, MALDI-TOF revolutionized proteomics, microbiology, and organic analysis by enabling mass determination of proteins and polymers exceeding 100 kDa.	Surface Plasmon Resonance (SPR) is a real-time, label-free technique for detecting and monitoring biomolecular interactions at a sensor surface by measuring changes in the refractive index caused by ligand binding. Developed by Kretschmann in 1971 and applied to biosensing by Liedberg, Nylander, and Lundström in 1983, SPR is now a gold standard for measuring binding kinetics (association and dissociation rates) and equilibrium binding constants in protein interactions, antibody-antigen recognition, and drug discovery.