Comparar métodos

	Cronoamperometría	RDE Koutecky-Levich	Resonancia de Plasmones Superficiales
Campo	Espectroscopia	Espectroscopia	Espectroscopia
Familia	Process / pipeline	Process / pipeline	Process / pipeline
Año de origen	1954	1962	1971
Autor original	Paul Delahay	Veniamin Levich	Erich Kretschmann
Tipo	Electrochemical technique	Electrochemical technique	Optical technique
Fuente seminal	Bard, A. J., & Faulkner, L. R. (2001). Electrochemical Methods: Fundamentals and Applications. John Wiley & Sons, 2nd edition.	Levich, V. G. (1962). Physicochemical Hydrodynamics. Prentice Hall.	Kretschmann, E. (1971). Determination of optical constants of metals by excitation of surface plasmons. Zeitschrift für Physik, 241(4), 313-324.
Alias	CA, chronoamperometric method	RDE, rotating disk electrode, Koutecky-Levich	SPR, surface plasmon, SPR biosensing
Relacionados	3	3	3
Resumen	Chronoamperometry (CA) is an electrochemical technique that measures current as a function of time when a potential step is applied to an electrode. Developed by Delahay in the 1950s, CA reveals diffusion-controlled electrochemical processes and enables determination of diffusion coefficients, surface coverage, and kinetic rate constants by analyzing the transient current decay.	Rotating Disk Electrode (RDE) electrochemistry combined with Koutecky-Levich analysis is a powerful electrochemical technique that decouples diffusion-limited and kinetically limited electron-transfer processes. Developed by Levich in the 1960s, RDE enables determination of heterogeneous electron-transfer rate constants and mechanistic information by rotating an electrode to control mass transport.	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.