Abstract
Furfural derivatives are present at high concentrations in many thermal processed foods. However, they are intensely known for their carcinogenic and genotoxic potential, being the impact of these compounds in a biological environment of paramount importance. Here, the interaction of the bovine serum albumin (BSA) and human transferrin (HTF) proteins with four furfural derivatives have been investigated. For this purpose, it has been used multi-spectroscopic methods together with theoretical tools. Results showed that Fur1 and Fur2 (keto derivatives) follow a dynamic mechanism for both proteins. Besides, the carboxyl derivative Fur3 suppressed the BSA and HTF fluorescence according to a static and dynamic mode, respectively. In contrast, the other carboxyl derivative Fur4 quenches the intrinsic fluorescence of both proteins according to a static mechanism. By one side, the best binder Fur4 attached very tightly to both proteins, while Fur3 has similar affinity to BSA as Fur4 but far less to HTF. On another side, Fur1 and Fur2 displayed weak affinities to BSA and also to HTF. Ultimately, the theoretical results of molecular docking revealed relevant aspects of favorite bind sites occupied by the furfural derivatives in the proteins.
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