Exploring The Interactions of a Natural Gamma-Oryzanol with Human Serum Albumin: Surface Plasmon Resonance, Fluorescence, and Molecular Modeling Studies
Drug Res (Stuttg) DOI: 10.1055/a-1533-2941γ-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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Source: Drug Research - Category: Drugs & Pharmacology Authors: Maleki, Somaiyeh Arabzadeh, AmirAhmad Nejati, Kazem Fathi, Farzaneh Tags: Original Article Source Type: research