Correction: Confocal Raman microspectroscopy for skin characterization: a comparative study between human skin and pig skin

Abstract

Correction for ‘Confocal Raman microspectroscopy for skin characterization: a comparative study between human skin and pig skin’ by Sana Tfaili et al., Analyst, 2012, 137, 3673–3682, DOI: 10.1039/C2AN16292J.

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The authors regret that the assignment of the Raman vibration at 1047 cm⁻¹ in Table 2 is incorrect in the original article. The correct version of Table 2 is shown below.

Table 2 Raman band assignment^a

SC surface		SC/epidermis		Epidermis
Transkin	Pig skin	Transkin	Pig skin	Transkin	Pig skin	Assignment
a γt: twisting (torsion), δ: bending or deformation, ν: stretching, ρ: rocking, A: adenine, C: cytosine, G: guanine, T: thymine.
427						Cholesterol^12
459	457	457		457		Polysaccharides^13
486		486		486		Glycogen^14
519		519				Phospholipids^13
529		529		527		ν(S–S) in keratin, ν(S–S) disulfide in proteins,^14,15 ceramides,^16 ν(S–S) gauche–gauche–trans (amino acid cysteine)^17
546	545	541		543		Glucose–saccharide band, cholesterol^17
564		564		564		Polysaccharides^13
		582		582		δ OH out of plane^18
597		597		597		Phospholipids^17
605		605	607	605		Glycerol^17
				619		γt C–C (protein)^19
624	622	624	622	624		γt C–C mode of phenylalanine (proteins)^14,15,20
646		646		646		γt C–C mode of tyrosine, cysteine^12
667		667		667		T, G (DNA/RNA)^20
701		701		701		ν(C–S) trans (amino acid methionine),^21 cholesterol, cholesterol ester^17
724		722		724		DNA^22
745		747	749	749		T (ring breathing mode of DNA/RNA bases),^19 DNA,^22 symmetric breathing of tryptophan (protein assignment)^12,14,15,23
803		803		803		Uracil-based ring breathing mode^24
829	828	828	826	828	827	Out-of-plane ring breathing, tyrosine (1^st peak of the Fermi doublet),^14,15 phosphodiester,^25 ν O–P–O DNA/RNA^20
854		854		854		Tyrosine (1^st peak of the Fermi doublet) and polysaccharide^26
897		898		896	898	Saccharide band,^17 monosaccharides (β-glucose), (C–O–C) skeletal mode,^25 phosphodiester, deoxyribose^21
		930				ν(C–C), probably in amino acids (protein band)^27
936	937	937		936	937	ν(C–C), α-helix (proteins), amino acid side chain vibrations^12
987		987		983		ν(C–C), β-sheet (proteins)^20
1003		1003		1003		Phenylalanine^12
1031		1031		1031		O–CH3 ν of methoxy groups^18
						δ(C–H), phenylalanine (protein assignment)
						Phenylalanine, ν(C–N) of proteins^23
1047						ν PO4^3−,^12 C–C and C–O stretching in HA
1062		1062	1059	1062		ν(C–C) skeletal, lipids^28
1082		1082		1082		ν(C–C) or v(C–O), phospholipids (lipid assignment),^23 phosphate vibrations (phosphodiester groups in nucleic acids),^29 nucleic acids^30
		1095		1095		Lipid,^31 ν(C–N),^12 phosphodioxy group in nucleic acids^20
1128		1128		1127	1129	ν(C–N),^32 ν(C–C) skeletal trans conformation,^33 phospholipid^34
1155		1155		1155		ν(C–C) & (C–N) of proteins (also carotenoids),^14,15 glycogen^30
1173	1175	1175		1173	1175	Cytosine, guanine^25
1207		1206	1205	1205		ν(C–C6H5), tryptophan, phenylalanine (protein assignment)^23,26
		1244		1244		One of the two most distinct peaks for RNA (with 813 cm^−1),^19 (C, T)^14
1255		1255		1256		Lipids^30 (doublet with the 1297 peak), amide III, adenine, cytosine^14
1271		1268	1271	1271		Amide III,^14 C–H (lipid)^29
				1294		Cytosine^25
1297		1299	1301	1302		δ CH2 lipid,^13 adenine, cytosine^14
				1309		γt CH3/CH2^21
1339		1336	1339	1338	1339	Nucleic acid mode^6,35
1389		1387		1389		CH3 band,^14 δ CH3 symmetric (lipid)^26
		1393		1393		CH rocking^20
1416						ν(C=O) of COO^− (amino acids aspartic & glutamic acid)^21
1442	1441					Cholesterol,^32 fatty acids,^30,37 δ CH2, δ CH3^38
		1449	1451	1449	1451	δ CH2, δ CH3,^12,29,38 C–H vibration (proteins), C–H vibration (lipids)^20
1526		1526		1526		–C=C– carotenoid^14
1545		1545		1546		Tryptophan^14,15
1561				1562		Tryptophan^27
1588		1585		1586		δ C=C mode of phenylalanine,^12,27 ν(C=C) olefinic (protein assignment)^26
1604		1604		1604		δ C=C in-plane mode of phenylalanine & tyrosine,^14,15 cytosine (NH2)^25
1613		1613		1613		Tyrosine^12
1652	1653	1653		1653		ν(C=O) amide I,^23 amide I α-helix,^39 lipid ν(C=C),^14,29 carbonyl ν(C=O)^24 and elastin (protein assignment)^23,26
1671		1671		1671		Amide I band (ν C=O coupled to a δ N–H),^17,40 ceramides^17
		1724		1724		ν(C=O)OH (amino acids aspartic & glutamic acid)^21
1742		1742		1742
2724		2727		2724		ν CH^41
2724		2727		2724		ν CH2 symmetric of lipids, ν CH3 symmetric of lipids^42
2849		2850		2849		ν CH2 asymmetric of lipids and proteins^42
2880		2880		2880		ν CH2 asymmetric of lipids and proteins^42
2889		2889		2889		ν CH2 asymmetric^42
2934		2934		2934		ν CH^43

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The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.

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