AI Article Synopsis
- The study investigates the formation of a stable protein corona using human α-1-acid glycoprotein (AGP) and citrate-stabilized silver nanoparticles (Ag-CIT), highlighting its significance in cellular responses to nanoparticles.
- The molecular docking simulations and experimental techniques demonstrated a strong interaction, with a high binding constant of 10 M, indicating AGP's ability to form a robust bioconjugate with the nanoparticles.
- Importantly, the formation of this AGP corona maintains the protein's native structure and reduces the cytotoxic effects of silver nanoparticles, enhancing their biocompatibility.
Article Abstract
Given the importance of protein corona in determining cellular responses to nanoparticles, numerous studies have been devoted to finding stable, biocompatible, and nontoxic protein corona. In this work, the interaction between human α-1-acid glycoprotein (AGP) and citrate-stabilized silver (Ag-CIT) nanoparticles of about 10 nm was methodically studied using molecular docking simulation approach and various experimental techniques. It could be shown that a stable Ag-CIT/AGP bioconjugate was formed with a high binding constant of 10 M, several orders of magnitude larger than that of other highly abundant serum proteins. Formation of AGP corona was accompanied by conserving the native conformation of the protein and further associated with a considerable decrease in the cytotoxicity of the silver nanoparticles.
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| http://dx.doi.org/10.1021/acs.langmuir.0c01018 | DOI Listing |
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