Table 2 SERS peak positions and the tentative vibrational assignments of the penguin brain tissue specimens under NIR (785 nm) excitation wavelength16,17,44,45,46,47,51,52,53,54,55,56.
Peak position (cm−1) | Assignments |
|---|---|
547 | Amino acids (tryptophan) combined with nucleobases DNA and RNA (cytosine and guanine) |
623 | C–C twisting mode of phenylalanine |
642 | C–C twisting mode of tyrosine |
661 | C–S stretching mode of cystine |
704 | CH2 rocking coupled with symmetric breathing of l-tyrosine |
719 | Symmetric choline C–N stretch (membrane phospholipid head) coupled with ring breathing mode of DNA/RNA nucleobases adenine |
744 | CH2 rocking coupled with symmetric breathing of tryptophan, mitochondria, and cytochrome c |
880 | Secondary amino acid proline |
964 | Hydroxyapatite (PO43− symmetric stretching)/carotenoid/cholesterol |
978 | C-H out-of-plane deformation coupled with C–C asymmetric stretching of Deoxygenated cells, cytochrome c, and porphyrin |
1003 | Symmetric C–C aromatic ring breathing mode of phenylalanine and collagen IV, and I |
1067 | C–C stretching coupled with C–C skeletal stretching, PO2 symmetric stretching of nucleic acid, protein, phospholipid, glycogen, and collagen IV |
1088 | |
1131 | C–N stretching in proteins |
1158 | C–C stretching of carotenoids coupled with C–N stretching of proteins |
1179 | C-H in-plane bending of hemoglobin, tyrosine, and flavin |
1273 | In-plane deformation of N–H, C–N stretching |
1305 | CH3 in-plane deformation of amide III |
1351 | CH3− (C=O) tryptophan, mitochondria, cytochrome c |
1384 | CH3 in-phase deformation, methyl symmetric bending of thymine, adenine, and guanine of DNA |
1399 | CH3 bending due to methyl bond in the membrane |
1448 | δ(CN) bending, δ(CH)3 out-of-phase deformation of lipid and protein |
1556 | C=C tryptophan, porphyrin |
1622 | C=C stretching mode of tyrosine and tryptophan |
1661 | Amide I (proteins with b-sheet conformational structures), ν(C=O), and collagen I, IV |