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Updated: Apr 27, 2026

Characterizing Cellular Proteins with In-cell Fast Photochemical Oxidation of Proteins
Published on: March 11, 2020
Surface characterization of oxidized myofibrils using X-ray photoelectron spectroscopy and scanning electron
Weizheng Sun1, Qingyun Li, Feibai Zhou
1College of Light Industry and Food Sciences, South China University of Technology , Guangzhou 510640, China.
Abstract:
The functional properties of myofibrils depend largely on their surface characteristics. Changes in surface characteristics of myofibrils after chemical oxidation were elucidated using X-ray photoelectron spectroscopy (XPS) and scanning electron microscopy. Myofibrils were oxidized by a hydroxyl radical generating system. Lipid oxidation and phospholipid distribution were altered during the oxidative processing. Results from particle size analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and salt solubility indicated that protein cross-linking and fragmentation occurred during the oxidation of myofibrils. XPS analysis of C 1s, N 1s, and O 1s spectra suggested that surface chemical function concentrations changed significantly because of the modification of amino acid side chains that rendered protein cross-links and fragmentation and phospholipid alteration. Analysis of the correlation between the surface chemical composition and parameters of particle size distributions confirmed that protein carbonylation and phospholipid alteration were involved in protein surface modification. Results of the microstructure analysis were in agreement with those of particle size and XPS analysis.
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