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Updated: Oct 14, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
Published on: March 13, 2014
Non-covalent complexes of Chlorella pyrenoidosa antioxidant peptides with chlorogenic acid: structure-activity
Zhiyi Chen1, Xingyue Jiang1, Guizhao Liang1
1Key Laboratory of Biorheological Science and Technology, Ministry of Education, Bioengineering College, Chongqing University, Chongqing, 400044, China.
Abstract:
Non-covalent complexation with chlorogenic acid (CA) was investigated to remodel complex-level structure-activity relationships of antioxidant peptides (AOPs) from Chlorella pyrenoidosa protein hydrolysates (CPPH) and to evaluate their potential cytoprotective interaction. CPPH-CA complex formation and conformational/microenvironmental changes were characterized by FTIR, intrinsic fluorescence, UV-vis, and interfacial/colloidal measurements. Antioxidant activity and synergy of CPPH-CA and peptide-CA systems were quantified using ABTS, DPPH, and FRAP assays. Representative AOPs were identified by LC-MS/MS and in silico screening, synthesized, and analyzed by quantum chemical parameters (HOMO/LUMO, ESP, ALIE, Fukui functions and IGMH). CA associated with AOPs mainly through hydrogen bonding and van der Waals forces, inducing charge redistribution and decreased HOMO-LUMO gaps, consistent with enhanced reactivity and synergy. In H2O2-injured HepG2 cells, PLR-CA exhibited a potential cytoprotective effect under the tested conditions by improving cell viability, reducing lipid peroxidation, and restoring antioxidant enzyme activities.
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