Journal
CARBOHYDRATE RESEARCH
Volume 346, Issue 7, Pages 949-955Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.carres.2011.02.005
Keywords
7-[3-Amino-4-O-(alpha-L-mycarosyl)-2,3,6-trideoxy-alpha-L-lyxo-hexopyranosyl]daunorubicinone; Human serum albumin; Fluorescence quenching; Molecular modeling; Synchronous fluorescence
Funding
- National Natural Science Foundation of China [20872029, 30970696]
- program for Innovative Research Team (in Science and Technology) in University of Henan Province [20081RTSTHN002]
- Innovation Scientists and Technicians Troop Construction Projects of Henan Province [084100510002]
Ask authors/readers for more resources
An improved synthetic approach to 7[3-amino-4-O-(alpha-L-mycarosyl)-2,3,6-trideoxy-alpha-L-lyxo-hexopyranosyl]daunorubicinone (alpha 1) 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 alpha 1 caused the fluorescence quenching of HSA by the formation of alpha 1-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 alpha 1-HSA complexes at room temperature was also discussed. All the experimental results and theoretical data indicated that alpha 1 bound to HSA and was effectively transported and eliminated in the body. Such findings may provide useful guidelines for further drug design. (C) 2011 Published by Elsevier Ltd.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available