Effect of (E,E)‐2,4‐decadienal on Side‐Chain Modification, Conformation Change, and Aggregation of Bovine Serum Albumin

Abstract

Protein modification by active aldehydes is associated with ageing and some chronic diseases, and it is closely related to food quality and safety. In this study, the modification of bovine serum albumin (BSA) using trans,trans-2,4-decadienal at various concentrations (0-10 mm) is investigated. The results show that the changes in the number of free amino groups and arginine residues, carbonyl formation, aggregation characteristics, and fluorescent lipofuscin-like pigments (LFLP) fluorescence are more severe at (E,E)-2,4-decadienal concentrations of 4-10 mm, whereas the conformational changes are more significant at low concentrations (0.1-2 mm). In the BSA modified by 1-10 mm (E,E)-2,4-decadienal, the microenvironment of tryptophan residues to become more hydrophobic, the structure became compact, hydrophobic binding sites decreases, molecular weight and particle size increases, and covalently cross-linked heterogeneous aggregates increases. At the same time, the relationship between the oxidation parameters and samples is explained using principal component analysis and hierarchical cluster analysis. Practical Applications: (E,E)-2,4-decadienal is highly electrophilically active with biomacromolecules. However, compared to the widely studied malonaldehyde (MDA), acrolein (ACR), 4-hydroxynonenal (HNE), and 4-oxo-trans-2-nonenal (ONE)-protein adducts, research on the modification of a protein by (E,E)-2,4-decadienal is insufficient, and the chemical nature of (E,E)-2,4-decadienal-protein adducts is not clear. This study may be useful for extending our understanding of the specific role of (E,E)-2,4-decadienal in the formation of modified proteins during the occurrence of chronic diseases and provides a theoretical reference for food quality and safety problems caused by protein carbonylation during processing and storage.

Self-Assembly of Precisely Fluorinated Albumin for Dual Imaging-Guided Synergistic Chemo–Photothermal–Photodynamic Cancer Therapy

“…Because of the weak interactions, albumin nanoparticles prepared through physical absorption are prone to dissociation and burst drug release under biological conditions . Although covalent bonds can significantly improve stability, unspecific modification, conjugation, and crosslink are usually used to construct albumin nanoparticles, leading to heterogeneous components and nanostructures, severely altered albumin structures and biological properties, and possible immunogenicity and toxicity. − Thus, the development of albumin nanoparticles through precise covalent modification without crosslink and heterogeneity may maximize the benefits of albumin as a natural vehicle for cancer drug delivery.…”