方法对比

	SERS	圆二色性	表面等离激元共振
领域	光谱学	光谱学	光谱学
方法族	Process / pipeline	Process / pipeline	Process / pipeline
起源年份	1974	1969	1971
提出者	Martin Fleischmann	Jean-Claude Fasman	Erich Kretschmann
类型	Vibrational spectroscopy technique	Spectroscopic method	Optical technique
开创性文献	Fleischmann, M., Hendra, P. J., & McQuillan, A. J. (1974). Raman spectra of pyridine adsorbed at a silver electrode. Chemical Physics Letters, 26(2), 163-166.	Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116.	Kretschmann, E. (1971). Determination of optical constants of metals by excitation of surface plasmons. Zeitschrift für Physik, 241(4), 313-324.
别名	Surface-enhanced Raman scattering, SERS spectroscopy	CD spectroscopy, circular dichroism, CD analysis	SPR, surface plasmon, SPR biosensing
相关	3	3	3
摘要	Surface-Enhanced Raman Spectroscopy (SERS) amplifies weak Raman signals by many orders of magnitude when analyte molecules are adsorbed on specially prepared metal (typically silver or gold) nanostructured surfaces. Discovered by Fleischmann, Hendra, and McQuillan in 1974, SERS enables detection of vibrational signatures of single molecules and ultra-trace contaminants, revolutionizing analytical chemistry and forensics.	Circular Dichroism (CD) spectroscopy measures the differential absorption of left- and right-circularly polarized light by optically active molecules, particularly proteins and nucleic acids. Introduced by Greenfield and Fasman in 1969, CD is a rapid, non-destructive technique for characterizing secondary structure (alpha-helix, beta-sheet), monitoring protein folding transitions, and assessing conformational changes in response to pH, temperature, or ligand binding.	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.