Drug Res (Stuttg)
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
1  Department of Biology, Faculty of Natural Sciences, University of Tabriz, Tabriz, Iran
,
AmirAhmad Arabzadeh
2  Department of Surgery, School of Medicine, Ardabil University of Medical Sciences, Ardabil, Iran
,
Kazem Nejati
3  Pharmaceutical Sciences Research Center, Ardabil University of Medical Sciences, Ardabil, Iran
,
Farzaneh Fathi
3  Pharmaceutical Sciences Research Center, Ardabil University of Medical Sciences, Ardabil, Iran
4  Biosensor Sciences and Technologies Research Center (BSTRC), Ardabil University of Medical Sciences, Ardabil, Iran
› Author Affiliations
Funding Research reported in this publication was supported by Ardabil University of Medical Sciences under grant number [4932], Ardabil, Iran.

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.

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Publication History

Received: 20 April 2021
Received: 02 June 2021

Accepted: 21 June 2021

Publication Date:
30 July 2021 (online)

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