Protein adsorption and drug delivery potential of graphitic carbon nitride nanorods: physicochemical insights with human serum albumin and quercetin

The two-dimensional polymeric material graphitic carbon nitride (gCN) has remarkable stability, with applications in photothermal therapy and drug delivery. When nanomaterials encounter proteins, they can lead to protein adsorption on their surfaces or the development of a protein corona. Such interactions could either influence or impair the biological roles of proteins. In this study, the time-dependent interaction between graphitic carbon nitride sheet-like nanorods (gCN NRs) and human serum albumin (HSA) was investigated to elucidate the molecular mechanism of protein adsorption and corona evolution. Steady-state and time-resolved fluorescence spectroscopy, circular dichroism spectroscopy, isothermal titration calorimetry and differential scanning calorimetry were employed to characterize the binding process, conformational changes, and thermodynamic aspects of the interaction. The results reveal that HSA initially binds to the surface of gCN NRs through weak interactions, with minimal conformational changes. However, the adsorbed protein continues to undergo structural rearrangements over time, leading to significant alterations in its secondary and tertiary structures. Furthermore, the drug loading and delivery of gCN NRs were studied with a hydrophobic drug, quercetin, which altered the surface properties of the nanorods and resulted in enhanced interaction with HSA. These findings provide mechanistic insights into the adsorption behaviour, conformational evolution, and protein corona formation of HSA on gCN NRs.

Abstract from PubMed (PMID 42969146). This entry was added automatically by our daily literature monitor because it matches the topics we follow; read the full paper at the original source.