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09 October 2020: Lab/In Vitro Research

Morphological and Biochemical Properties of Human Astrocytes, Microglia, Glioma, and Glioblastoma Cells Using Fourier Transform Infrared Spectroscopy

Dongsheng Kong 1BEF* , Wenyu Peng 2CDF* , Rui Zong 1ABG* , Gangqiang Cui 3BCD , Xinguang Yu 1AG*

DOI: 10.12659/MSM.925754

Med Sci Monit 2020; 26:e925754

Table 1 Assignment of the most prominent absorption bands.

Peak IDBand/cm−1Assignment
1965–980C-C, PO-stretch: DNA, RNA, phospholipids
21039C-O-H deformation: glycogen
31070–1150C-O-C and C-C stretch: carbohydrates, lipids, glycolipids
41083–1085PO-symmetric stretch: nucleic acids in DNA and RNA
51172C-O (H) stretch: carbohydrates
61237–1244PO-asymmetric stretch: nucleic acids, lipids
71277C-H/N-H deformation: amide III, components of proteins
81393–1402-COO-symmetric stretch: fatty acids, amino acids
91450–1454CH, CH deformation: mainly lipids, proteins
101538–1546N-H bend (60%), C-N stretch (40%) and C-C stretch: amide II, peptide, proteins (α-helix, β-sheets, turn and random coil)
111600–1706C=O stretch (76%), C-N stretch (14%), CNN (10%): amide I, proteins (α-helix, β-sheets, turn and random coil)
121746C=O stretch: esters (lipids, phospholipids)
131700–1799C=O deformation: lipids
142844–2860-CH symmetric stretch: lipids
152892–2924-CH symmetric stretch: lipids
162953–2994-CH asymmetric stretch: lipids
173099–3296-NH symmetric stretch: amide B, peptides, proteins
183327–3337-NH asymmetric stretch: amide A, peptides, proteins

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Medical Science Monitor eISSN: 1643-3750
Medical Science Monitor eISSN: 1643-3750