Hydroxyl radical induced structural changes of collagen
Open accessAbstract
Extracellular matrix (ECM) plays an important role in cell differentiation, growth, migration and apoptosis. Collagen is the most abundant protein family in vivo , but its function has still not been clearly defined yet. Reactive oxygen species (ROS) have a central role in oxidative cell stress. Electron spin resonance (ESR) spectroscopy indicates that type I collagen could uniquely scavenge hydroxyl radicals in dose‐ and time‐dependent manner; whereas BSA and gelatin (a denatured collagen) have no such an effect. However, the mechanism by which type I collagen scavenges hydroxyl radicals is different from that of GSH, a well‐known free radical scavenger. Using a new method, two‐dimensional FTIR correlation analysis, for the first time, we show that the order of functional group changes of type I collagen in this process is amide I earlier than amide II than amide III than –CH– than ν (C=O). The results indicates that the structure of the main chain of collagen changed first, followed by more residue group ν (C=O) exposed to hydroxyl radicals. The reaction with the carbonyl group in collagen causes the hydroxyl free radicals to be scavenged. Therefore, ECM can effectively scavenge ROS under normal physiological conditions. When the proteins of ECM were denatured in the same way as gelatin, they lost their function as a free radical scavenger. All of these results provide new insight into therapy or prevention of oxidative stress, apoptosis and ageing.
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The FTIR spectrum of pure type I collagen exhibits characteristic absorption bands: amide I at approximately 1642 cm−1, amide II at 1537 cm−1, and amide III at 1236 cm−1.
“The strong band centered at approximately 1642 cm⁻¹ is assigned to the amide I vibration, predominantly arising from C=O stretching of the peptide backbone and highly sensitive to collagen secondary structure.”
From Montmorillonite-reinforced methacrylated collagen/methacrylated silk fibroin hydrogel-based inks: rheological and physicochemical characterization for bone scaffold applications (2026) · cites this paper as [34]
Section 3.2 identifies an amide I band at 1640 cm⁻¹, supporting the citing sentence’s assignment near 1642 cm⁻¹. But the fuller attributed claim gives amide II at 1537 cm⁻¹, whereas section 3.2 reports 1547 cm⁻¹; section 3.3 places amide III near 1239 rather than 1236 cm⁻¹. The paper therefore supports the band identities, but not all three stated positions. (LLM, conf=0.86)
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- Authors
- Xiao, H., Cai, G., & Liu, M.
- Affiliations
- University of Toronto (CA)
- Tsinghua University (CN)
- Corresponding author
- Cai, Guoping
- ORCID
- Liu, Mingyao
- Venue
- Journal of Spectroscopy
- Publisher
- Wiley
- Published
- 2007-01
- Volume
- 21
- Issue
- 2
- Pages
- 91-103
- ISSN
- 2314-4920 (ISSN-L)
- 2314-4939
- OpenAlex
- W2124731793
- Cited by
- 28
- References
- 41
- Citations by year
- 2026: 9 · 2025: 3 · 2024: 3 · 2023: 2 · 2022: 2 · 2021: 3 · 2016: 2 · 2013: 1
- FWCI
- 0.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Spectroscopy (publishedVersion, cc-by)
- TSpace (University of Toronto) (submittedVersion, cc-by)
- Funders
- Tsinghua University
- Topics
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Spectroscopy Techniques in Biomedical and Chemical Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Electron Spin Resonance Studies
- Keywords
- type I collagen, hydroxyl radical scavenging, reactive oxygen species, extracellular matrix, collagen denaturation, gelatin, oxidative stress, apoptosis, aging
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