Binding behavior of 6PPD and its oxidation product 6PPD-quinone with albumin protein: Mechanistic insights into toxicity assessment
• The binding mechanisms between 6PPD/6PPD-Q and albumin were demonstrated. • 6PPD/6PPD-Q spontaneously interacted with albumin to form complexes. • Bound albumin greatly inhibited the cellular uptake of harmful 6PPD/6PPD-Q. • Binding of albumin to 6PPD/6PPD-Q reduced ROS formation and cytotoxicity. • Cytotoxicity of 6PPD and its alternatives was inversely related to their binding affinities with albumin.
Authors
- Naihao Lu (ORCID: https://orcid.org/0000-0003-3336-2502)
- Shi-Ya Peng
- Rong Tian
- Die Wen
Institutions
- Jiangxi Normal University (CN)
Publication Details
- Journal
- Industrial Crops and Products
- Published
- 2026-05-29
- DOI
- https://doi.org/10.1016/j.indcrop.2026.123586
- Primary Topic
- Protein Interaction Studies and Fluorescence Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China