A Facile Access to Green Fluorescent Albumin Derivatives

A Morita‐Baylis‐Hillman Adduct (MBHA) derivative bearing a triphenylamine moiety was found to react with human serum albumin (HSA) shifting its emission from the blue to the green‐yellow thus leading to green fluorescent albumin (GFA) derivatives and enlarging the platform of probes for aggregation‐induced fluorescent‐based detection techniques. A possible interaction of MBHA derivative 7 with a lipophilic pocket within the HSA structure was suggested by docking studies. DLS experiments showed that the reaction with HSA induce a conformational change of the protein contributing to the aggregation process of GFA derivatives. The results of investigations on the biological properties suggested that GFA retained the ability of binding drug molecules such as warfarin and diazepam. Finally, cytotoxicity evaluation studies suggested that, although the MBHA derivative 7 at 0.1 μg/mL affected the percentage of cell viability in comparison to the negative control, it cannot be considered cytotoxic, whereas at all the other concentrations≥0.5 μg/mL resulted cytotoxic at different extent. A Morita‐Baylis‐Hillman Adduct derivative bearing a triphenylamine moiety is capable of reacting with human serum albumin shifting its emission from the blue to the green‐yellow, leading to green fluorescent albumin (GFA) derivatives, and enlarging the platform of probes for fluorescent‐based detection techniques. The results of investigations on the biological properties suggest that GFA retains the ability of binding drug molecules.