Research Article

Determination of the Immunoglobulin G Spectrum by Surface-Enhanced Raman Spectroscopy Using Quasispherical Gold Nanoparticles

Table 1

Characteristic Raman bands of IVIG.

Raman shift (cm-1)Proposed band assignmentReference

710Tyrosine (642, 640-650)[17]
Tryptophan (707)-in IgG-[18]
852Carbon backbone v (Cα-C, Cα-Cβ y Cα-N) (870-1150)[19]
Glycine, alanine v (CNC) (850-900) assigned to the symmetric CNC stretch mode[20]
Tyrosine (852)-in IgG-[21]
Tyrosine (843) v (ring)-in IgG-[18]
Tyrosine out of plane ring bending mode at 853[22]
Hydrogen bonding state of tyrosine[23]
1001Phenylalanine (1003, 1000-1010)[17, 23]
Symmetric breathing mode of phenylalanine (1003)[22]
1130Cysteine (CH bend) (1142)[20]
Glutamine (1122) (NH3 bend and rock modes)[20]
1237Amide III region (1230-1340) δ (N-H, Cα-H), v (Cα-N)[19]
β-Sheet structure (1239)[24]
β-sheet structure, amide III (1230-1240)[23]
Glutamine (1225) (CH2 bend and twist)[20]
Tryptophan, tyrosine δ (ring) (1225)-in IgG-[18]
Amide III, β-sheet and random coils (1242)[25]
1396Histidine (1400-1420)[17]
Tryptophan v ring stretching-in IgG-(1366)[21]
Tyrosine v (ring) (1385)-in IgG-[18]
Glycine (1411) CH2 scissor mode[20]
1449Tryptophan CH2 scissors-in IgG-[21]
Tryptophan or δ (CH2) (1455)-in IgG-[18]
Glutamine (CH2 bend and scissors modes) (1462)[20]
C-H vibration (1449); CH functional groups in amino acid side chains of proteins[25]
1497Glycine (CH2 and OH bending modes) (1495)[20]
Tryptophan, tyrosine v (ring) (1487)-in IgG-[18]

δ: deformation; v: stretching.