Experimental and computational studies of the interactions of a novel fusarochromanone analog with DNA and human serum albumin

Abstract

Drugs are primarily transported to target tissues by plasma proteins, including human serum albumin (HSA). HSA is the most abundant protein in human blood plasma, and it plays an important role as a carrier for various substances, including drugs, dyes, and ions. Hence, the analysis of drug-HSA interactions is pharmacologically important in drug development, which requires a thorough understanding of interactions at the cellular and molecular levels. Many anticancer drugs also exert their biological activity by interacting with DNA. This study investigates the interaction of a fusarochromanone analog (FC101g), a potential anticancer drug with both DNA and HSA through experimental assays and in silico docking methods. The results demonstrate that FC101g exhibits hydrophobic interactions with subdomains IA and IB in HSA binding domain I. The positive values of ΔS and ΔH indicate that van der Waals interactions and hydrogen bonds primarily constitute these interactions. The results also indicate that the fluorescence extinction of FC101g by DNA is a static quenching process, and the relevant binding forces consist of van der Waals interactions and hydrogen bonding. The molecular modeling results show that FC101g binds within the minor groove of DNA. These results may be useful in pharmacology and medicinal chemistry and provide new insights for future studies.