Add time:08/21/2019         Source:sciencedirect.com

An improved synthetic approach to 7-[3-amino-4-O-(α-l-mycarosyl)-2,3,6-trideoxy-α-l-lyxo-hexopyranosyl]daunorubicinone (α1) with high stereoselectivity and good yield was developed. The feature of its binding to human serum albumin (HSA) was also investigated under simulative physiological conditions via fluorescence and UV–vis absorption spectroscopy and molecular modeling methods. The results revealed that α1 caused the fluorescence quenching of HSA by the formation of α1–HSA complexes. Hydrophobic interactions played a major role in stabilizing the complex, which was in good agreement with the results of the molecular modeling study. In addition, the effect of common ions on the binding constants of α1–HSA complexes at room temperature was also discussed. All the experimental results and theoretical data indicated that α1 bound to HSA and was effectively transported and eliminated in the body. Such findings may provide useful guidelines for further drug design.

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