“…Specifically, BSA shows seven characteristic peaks at 617, 650, 1219, 1355, 1499, 1522, and 1650 cm –1 , which could be attributed to C–C twisting, OH out-of-plane bending, the amine III of proteins, tryptophan, CC stretching in a benzenoid ring, carotene, and amide I, respectively. − These peaks are almost missing in the case of LYS and OVA. Six peaks that were observed in SERS spectra of OVA are assigned to tryptophan, collagen, d(CH), υs COO – (IgG), CC stretching in benzenoid ring, and protein amide I absorption from left to right, respectively. − SERS features from LYS were also distinguishable from two other proteins. They are dominated by the bands of amino acids, such as the C–S stretching mode of cysteine, proline, phenylalanine, tyrosine, and amide I band of proteins, due to CO stretching (at 653, 825, 1032, 1164, and 1600 cm –1 , respectively). , These differences may be correlated with different amino acid species and protein spatial structures and, therefore, produce a signature pattern that allows us to distinguish three proteins.…”