Spectroscopic investigation of the anticancer alkaloid piperlongumine binding to human serum albumin from the viewpoint of drug delivery

Piperlongumine (PL) is a very promising natural agent with a high potential for cancer treatment. To overcome the poor water solubility of PL, there is a need to develop a novel water‐soluble formulation in which PL is non‐covalently bound to human serum albumin (HSA). PL binding to HSA was studied...

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Bibliographic Details
Published in:Luminescence (Chichester, England) England), 2018-03, Vol.33 (2), p.305-311
Main Authors: Liu, Yu, Li, Qian‐Yu, Wang, Yu‐Ping, Liu, Yi‐Ming, Liu, Bin, Liu, Mei‐Mei, Liu, Bing‐Mi
Format: Article
Language:English
Subjects:
Albumin
Alkaloids - chemistry
Antineoplastic Agents - chemistry
Binding sites
Cancer
carrier
Circular Dichroism
Dioxolanes - chemistry
Drug delivery
Drug Delivery Systems
Entropy
Forces (mechanics)
Human serum albumin
Humans
Hydrophobicity
Kinetics
piperlongumine
Protein Binding
Serum
Serum albumin
Serum Albumin, Human - chemistry
Solubility
Spectroscopic techniques
Stabilizing
Temperature
Temperature dependence
Thermodynamics
Warfarin
Water treatment
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Summary:Piperlongumine (PL) is a very promising natural agent with a high potential for cancer treatment. To overcome the poor water solubility of PL, there is a need to develop a novel water‐soluble formulation in which PL is non‐covalently bound to human serum albumin (HSA). PL binding to HSA was studied by various spectroscopic techniques under simulated physiological conditions. Spectroscopic evidence showed that the interaction of PL with HSA could form a PL–HSA complex. The binding constant (Ka) values increased with increasing temperature, and a similar dependence was observed for the number of binding sites (n) values. The number of PL molecules bound to HSA reached 8.1 when the temperature was raised to 308 K. Thermodynamic calculation results suggested that the binding reaction occurred spontaneously but was an entropy‐driven process, and hydrophobic forces played a major role in stabilizing the complex. Furthermore, PL binding induced conformational and microenvironmental changes in HSA. Displacement studies indicated that PL and warfarin had separate binding regions in site I. Therefore, it would be possible to develop a novel water‐soluble formulation involving PL and HSA. This study may provide some valuable information in terms of improving the poor water solubility of PL.
ISSN:1522-7235
1522-7243
DOI:10.1002/bio.3414