An investigation into the interaction between piplartine (piperlongumine) and human serum albumin

Piplartines are alkaloid amides present in the roots and stems of different pepper species which have promising pharmacological properties including cancer prevention. Some recent studies have determined pharmacokinetic parameters of piplartine in rat blood plasma but without pointing to any molecul...

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Published in:Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy Molecular and biomolecular spectroscopy, 2019-09, Vol.220, p.117084, Article 117084
Main Authors: de Alcântara-Contessoto, Nayara Sousa, Caruso, Ícaro Putinhon, Bezerra, Daniel Pereira, Filho, José Maria Barbosa, Cornélio, Marinônio Lopes
Format: Article
Language:English
Subjects:
Fluorescence spectroscopy
Human serum albumin
Molecular docking
Piperlongumine
Piplartine
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Summary:Piplartines are alkaloid amides present in the roots and stems of different pepper species which have promising pharmacological properties including cancer prevention. Some recent studies have determined pharmacokinetic parameters of piplartine in rat blood plasma but without pointing to any molecular target or describing the physicochemical forces of the interaction. The present study investigated the interaction between piplartine and human serum albumin (HSA) the predominant protein in blood plasma. Fluorescence spectroscopy was utilized to observe the complex HSA-piplartine formation. Thermodynamic parameter analysis indicates that the process occurs spontaneously and is enthalpically driven; the affinity constant suggests that this interaction is reversible. This was reinforced by the binding density function method and by the displacement analysis that the piplartine binds on HSA at a single site, which was determined to be the IIA sub-domain. In silico analysis (molecular docking) identified the main residues involved in binding and the corresponding forces, which corroborates well with the experimental results. [Display omitted] •Interaction PPTN into albumin detected by fluorescence spectroscopy has a suppression effect and unveiled as a static process•Drug displacement procedures helped to recognize site 1 in HSA as the preferential site of PPTN.•Thermodynamic parameters suggested a greater influence of enthalpy than of entropy for complex PPTN-HSA formation.•Thermodynamic parameters indicate that the forces present to build the complex were hydrogen bonds and van der Waals•Computational simulations confirmed the experimental results
ISSN:1386-1425
DOI:10.1016/j.saa.2019.04.076