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Insight into the interaction of inhaled corticosteroids with human serum albumin: A spectroscopic-based study

Journal of Pharmaceutical Analysis 2018年第1期8卷 37-44页

作者： carlotta pontremoli Nadia Barbero Guido Viscardi Sonja Visentin Department of Applied Science and Technology (DISAT) Politecnico of Torino Department of Chemistry and NIS Interdepartmental Centre University of Torino Molecular Biotechnology and Health Sciences Department University of Torino

It is well known that the safety and efficacy profile of an inhaled cortocosteroid(ICS) is influenced by the pharmacokinetic properties and associated pharmacodynamic effects of the drug. Freely circulating,protein unbound, and active ICS can cause systemic adverse effects. Therefore, a detailed investigation of drug-protein interaction could be of great interest to understand the pharmacokinetic behaviour of corticosteroids and for the design of new analogues with effective pharmacological properties. In the present work, the interaction between some corticosteroids and human serum albumin(HSA) has been studied by spectroscopic approaches. UV–Vis spectroscopy confirmed that all the investigated corticosteroids can bind to HSA forming a protein-drug complex. The intrinsic fluorescence of HSA was quenched by all the investigated drugs, which was rationalized in terms of a static quenching mechanism. The thermodynamic parameters determined by the Van't Hoff analysis of the binding constants(negative ΔH and ΔS values) clearly indicate thathydrogen bonds and van der Waals forces play a major role in the binding process between albumin and betamethasone, flunisolide and prednisolone, while hydrophobic forces may play a major role in stabilizing albumin-triamcinolone complexes.

关键词： Human serum albumin Inhaled corticosteroids Fluorescence spectroscopy Fluorescence resonance energy transfer(FRET)

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