Application of second derivative spectroscopy for increasing molecular specificity of fourier transform infrared spectroscopic imaging of articular cartilage
Open accessAbstract
Objective Fourier transform infrared (FT-IR) spectroscopic imaging is a promising method that enables the analysis of spatial distribution of biochemical components within histological sections. However, analysis of FT-IR spectroscopic data is complicated since absorption peaks often overlap with each other. Second derivative spectroscopy is a technique which enhances the separation of overlapping peaks. The objective of this study was to evaluate the specificity of the second derivative peaks for the main tissue components of articular cartilage (AC), i.e., collagen and proteoglycans (PGs).Materials and methods Histological bovine AC sections were measured before and after enzymatic removal of PGs. Both formalin-fixed sections (n = 10) and cryosections (n = 6) were investigated. Relative changes in the second derivative peak heights caused by the removal of PGs were calculated for both sample groups.Results The results showed that numerous peaks, e.g., peaks located at 1202 cm(-1) and 1336 cm(-1), altered less than 5% in the experiment. These peaks were assumed to be specific for collagen. In contrast, two peaks located at 1064 cm(-1) and 1376 cm(-1) were seen to alter notably, approximately 50% or more. These peaks were regarded to be specific for PGs. The changes were greater in cryosections than formalin-fixed sections.Conclusions The results of this study suggest that the second derivative spectroscopy offers a practical and more specific method than routinely used absorption spectrum analysis methods to obtain compositional information on AC with FT-IR spectroscopic imaging.
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Second derivative spectroscopy enables accurate measurements of wavelength position by identifying small and overlapping peaks that are not resolved in the original spectra.
“SD spectroscopy enables accurate measurements of wavelength position by identifying small and overlapping peaks that are not resolved in the original spectra. [23,46,47].”
From Response to nutrient variation on lipid productivity in green microalgae captured using second derivative FTIR and Raman spectroscopy (2022) · cites this paper as [46]
According to Beer Lambert's law, absorbance (FTIR and its derivatives SD-FTIR) is proportional to the analyte concentration.
“According to Beer L ambert's law, absorbance [(FTIR) and its derivatives (SD-FTIR)] is proportional to the analyte concentration [45,46].”
From Response to nutrient variation on lipid productivity in green microalgae captured using second derivative FTIR and Raman spectroscopy (2022) · cites this paper as [46]
Spectral intensity variation due to biomolecular transitions can be attributed to cell metabolism during growth phases.
“Thus the intensity variation observed in the spectra due to biomolecular transitions can be attributed to the metabolism of cells during their various phases of growth [26,28].”
From Biomolecular transitions and lipid accumulation in green microalgae monitored by FTIR and Raman analysis (2020) · cites this paper as [28]
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References 46 · Cited by 254
Research works printed but not linked: 3
- Camacho NP, West P, Torzilli PA, Mendelsohn R. FTIR micro- scopic imaging of collagen and proteoglycan in bovine carti- lage. Biopolymers 2001;62:1e8.
- Potter K, Kidder LH, Levin IW, Lewis EN, Spencer RG. Imaging of collagen and proteoglycan in cartilage sections using Fourier transform infrared spectral imaging. Arthritis Rheum 2001;44:846e55.
- Mark H, Workman J. Derivatives in spectroscopy Part II e the true derivative. Spectroscopy 2003;18:25e8.
- Authors
- Rieppo, L., Saarakkala, S., Närhi, T., Helminen, H. J., Jurvelin, J. S., & Rieppo, J.
- Affiliations
- University of Eastern Finland (FI)
- University of Oulu (FI)
- Corresponding author
- Rieppo, L.
- Saarakkala, S.
- Närhi, T.
- Helminen, H.J.
- Jurvelin, J.S.
- Rieppo, J.
- Venue
- Osteoarthritis and Cartilage
- Publisher
- Elsevier BV
- Published
- 2012-05
- Volume
- 20
- Issue
- 5
- Pages
- 451-459
- ISSN
- 1063-4584 (ISSN-L)
- OpenAlex
- W2008209064
- Cited by
- 254
- References
- 46
- Citations by year
- 2026: 14 · 2025: 26 · 2024: 19 · 2023: 20 · 2022: 22 · 2021: 36 · 2020: 22 · 2019: 19 · 2018: 18 · 2017: 14 · 2016: 20 · 2015: 8 · 2014: 7 · 2013: 5 · 2012: 2
- FWCI
- 3.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Osteoarthritis and Cartilage (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Finland
- Academy of Finland
- University of Oulu
- National Doctoral Programme of Musculoskeletal Disorders and Biomaterials; North Savo Regional Fund of The Finnish Cultural Foundation
- Instrumentarium Science Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Spectroscopy Techniques in Biomedical and Chemical Research
- Physical Sciences › Chemistry › Analytical Chemistry › Spectroscopy and Chemometric Analyses
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Optical Imaging and Spectroscopy Techniques
- Keywords
- second derivative spectrophotometry, articular cartilage, collagen, proteoglycans, peak overlap, bovine cartilage, frozen section, cartilage composition
- MeSH terms
- Animals, Cartilage, Articular, Cattle, Fixatives, Formaldehyde, Male, Proteoglycans, Cryopreservation, Tissue Fixation, Spectroscopy, Fourier Transform Infrared, Collagen Type II
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