<abstract xmlns="http://www.w3.org/1999/xhtml"><p>Calf skin collagen and three amino acids essential for its structure, namely glycine, L-proline and 4-hydroxyl-L-proline, were irradiated with gamma rays up to a dose of 10 kGy. Conversion of radicals over time or after thermal annealing to selected temperatures was monitored by X-band electron paramagnetic resonance (EPR) spectroscopy. Some experimental spectra were compared with signals simulated based on literature data from the electron nuclear double resonance (ENDOR) studies. The following phenomena were confirmed in the tested amino acids: abstraction of hydrogen atom (glycine, proline, hydroxyproline, collagen), deamination (glycine, hydroxyproline), decarboxylation (hydroxyproline). Chain scission at glycine residues, radiation-induced decomposition of side groups and oxidative degradation were observed in irradiated collagen. The decay of radicals in collagen saturated with water occurred at lower temperatures than in macromolecules having only structural water. The paramagnetic centres were the most stable in an oxygen-free atmosphere (vacuum). Radical processes deteriorated the structure of collagen; hence, radiation sterilization of skin grafts requires careful pros and cons analysis.</p></abstract>

Calf skin collagen and three amino acids essential for its structure, namely glycine, L-proline and 4-hydroxyl-L-proline, were irradiated with gamma rays up to a dose of 10 kGy. Conversion of radicals over time or after thermal annealing to selected temperatures was monitored by X-band electron paramagnetic resonance (EPR) spectroscopy. Some experimental spectra were compared with signals simulated based on literature data from the electron nuclear double resonance (ENDOR) studies. The following phenomena were confirmed in the tested amino acids: abstraction of hydrogen atom (glycine, proline, hydroxyproline, collagen), deamination (glycine, hydroxyproline), decarboxylation (hydroxyproline). Chain scission at glycine residues, radiation-induced decomposition of side groups and oxidative degradation were observed in irradiated collagen. The decay of radicals in collagen saturated with water occurred at lower temperatures than in macromolecules having only structural water. The paramagnetic centres were the most stable in an oxygen-free atmosphere (vacuum). Radical processes deteriorated the structure of collagen; hence, radiation sterilization of skin grafts requires careful pros and cons analysis.

Radicals initiated by gamma rays in selected amino acids and collagen

Institute of Nuclear Chemistry and Technology

Nukleonika

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

{"article-title":"Radicals initiated by gamma rays in selected amino acids and collagen"}

Calf skin collagen and three amino acids essential for its structure, namely glycine, L-proline and 4-hydroxyl-L-proline, were irradiated with gamma rays up to...

Radicals initiated by gamma rays in selected amino acids and collagen

Publié en ligne: 02 mars 2019

Pages: 11 - 17

Reçu: 12 nov. 2018

Accepté: 28 déc. 2018

DOI: https://doi.org/10.2478/nuka-2019-0002

Mots clés
amino acid, collagen, EPR spectroscopy, gamma rays

© 2019 Grażyna Przybytniak et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Radicals initiated by gamma rays in selected amino acids and collagen

Publié en ligne: 02 mars 2019

Pages: 11 - 17

Reçu: 12 nov. 2018

Accepté: 28 déc. 2018

DOI: https://doi.org/10.2478/nuka-2019-0002

Mots clésamino acid, collagen, EPR spectroscopy, gamma rays

© 2019 Grażyna Przybytniak et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Mots clés
amino acid, collagen, EPR spectroscopy, gamma rays