Oxidative fragmentation of collagen and prolyl peptide by Cu (II)/H2O2. Conversion of proline residue to 2-pyrrolidone
Open accessAbstract
Oxidative degradation of collagen and the model peptides by Cu(II)/H2O2 has been studied. The depolymerization of collagen was predominantly observed by use of gel filtration chromatography. Polyproline was used as a model for collagen, and the oxidative modification was examined by amino acid analysis. Glutamic acid and gamma-aminobutyric acid were identified in the hydrolysates of oxidized polyproline. The formation of glutamic acid was reduced by treatment with NaBH4. The model peptide, (Pro-Pro-Gly)10, was also degraded by Cu(II)/H2O2, and a new N-terminal glycine was generated in proportion to the reaction time. Hydroxyl radical scavengers show only partial inhibition of the degradation of (Pro-Pro-Gly)10. In order to estimate the fragmentation mechanism, we used N-tert-butoxycarbonyl (Boc)-L-prolylglycine as a model for collagen and (Pro-Pro-Gly)10. The degradation products were isolated and characterized. Then N-tert-Boc-2-pyrrolidone, which provides gamma-aminobutyric acid by acid hydrolysis, was identified. The formation of a 2-pyrrolidone compound from oxidized Boc-L-prolylglycine is direct evidence for the scission of the peptide bond. The time-dependent formation of N-tert-Boc-2-pyrrolidone and liberation of glycine from N-tert-Boc-L-prolylglycine exposed to Cu(II)/H2O2 was observed. These results suggest that the cleavage of the peptide bond (Pro-Gly) was caused by oxidation of the proline residue, which led to the formation of the 2-pyrrolidone compound. We confirmed that proline oxidation leads to the fragmentation of proteins, accompanied by the formation of a 2-pyrrolidone structure.
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- Authors
- Kato, Y., Uchida, K., & Kawakishi, S.
- Affiliations
- Nagoya University (JP)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-11
- Volume
- 267
- Issue
- 33
- Pages
- 23646-23651
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1571355387
- Cited by
- 71
- References
- 23
- Citations by year
- 2024: 2 · 2023: 1 · 2021: 1 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 3
- FWCI
- 2.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- collagen, proline oxidation, pyrrolidinone, peptide bond cleavage, polyproline, GABA, glutamate, hydroxyl radicals, protein fragmentation
- MeSH terms
- Amino Acid Sequence, Borohydrides, Chromatography, High Pressure Liquid, Collagen, Copper, Female, Humans, Hydrogen Peroxide, Indicators and Reagents, Kinetics, Mannitol, Molecular Sequence Data, Peptides, Placenta, Pregnancy, Proline, Pyrrolidinones, Time Factors
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