Exploring The Interactions of a Natural Gamma-Oryzanol with Human
                    Serum Albumin: Surface Plasmon Resonance, Fluorescence, and Molecular Modeling
                    Studies

Somaiyeh Maleki; AmirAhmad Arabzadeh; Kazem Nejati; Farzaneh Fathi

doi:10.1055/a-1533-2941

Drug Research, Table of Contents

Drug Res (Stuttg) 2021; 71(09): 520-527
DOI: 10.1055/a-1533-2941

Original Article

Exploring The Interactions of a Natural Gamma-Oryzanol with Human Serum Albumin: Surface Plasmon Resonance, Fluorescence, and Molecular Modeling Studies

Somaiyeh Maleki

¹Department of Biology, Faculty of Natural Sciences, University of Tabriz, Tabriz, Iran

,

AmirAhmad Arabzadeh

²Department of Surgery, School of Medicine, Ardabil University of Medical Sciences, Ardabil, Iran

,

Kazem Nejati

³Pharmaceutical Sciences Research Center, Ardabil University of Medical Sciences, Ardabil, Iran

,

Farzaneh Fathi

³Pharmaceutical Sciences Research Center, Ardabil University of Medical Sciences, Ardabil, Iran

⁴Biosensor Sciences and Technologies Research Center (BSTRC), Ardabil University of Medical Sciences, Ardabil, Iran

› Author Affiliations

Abstract

γ-oryzanol (ORY) is the vital bioactive compound, which is a mixture of ferulic acid ester and plant sterols. In the present work, the binding of ORY to human serum albumin (HSA) was investigated at the molecular level using fluorescence spectroscopy and surface plasmon resonance (SPR) as well as molecular modeling studies. Based on the fluorescence data analysis, ORY can form a non-fluorescent complex with HSA and induce static quenching of the emission intensity of HSA. Also, the high value of K _SV (34.69 × 10⁴ M⁻¹) confirmed a high sensitivity of HSA toward ORY. The real-time monitoring of the binding of ORY to HSA was carried out using the SPR technique. The small K _D value (1.23 × 10⁻⁶ M) calculated by SPR analysis indicated a high affinity of ORY toward HSA. The molecular modeling studies confirmed that ORY has only one binding site on HSA and binds HSA in a cavity between subdomain IIA and IIIA.

Key words

Human serum albumin - γ-oryzanol - Surface plasmon resonance - Static quenching mechanism - Molecular docking

Full Text

References

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