Binding properties of food colorant allura red with human serum albumin in vitro
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Allura red (AR) is a widely used colorant in food industry, but may have a potential security risk. In this study, the properties of interaction between AR and human serum albumin (HSA) in vitro were determined by fluorescence, UV–Vis absorption and circular dichroism (CD) spectroscopy combining with multivariate curve resolution–alternating least squares (MCR–ALS) chemometrics and molecular modeling approaches. An expanded UV–Vis data matrix was resolved by MCR–ALS method, and the concentration profiles and pure spectra for the three reaction components (AR, HSA, and AR–HSA complex) of the system were then successfully obtained to evaluate the progress interaction of AR with HSA. The calculated thermodynamic parameters indicated that hydrogen binding and hydrophobic interactions played major roles in the binding process, and the interaction induced a decrease in the protein surface hydrophobicity. The competitive experiments revealed that AR mainly located in Sudlow’s site I of HSA, and this result was further supported by molecular modeling studies. Analysis of CD spectra found that the addition of AR induced the conformational changes of HSA. This study have provided new insight into the mechanism of interaction between AR and HSA.
KeywordsAllura red Human serum albumin Binding mode Multivariate curve resolution–alternating least squares Molecular modeling
We gratefully acknowledge the financial support of the National Natural Science Foundation of China (Nos. 31060210 and 21167013), the Research Program of State Key Laboratory of Food Science and Technology, Nanchang University (Nos. SKLF–ZZB–201305, SKLF–ZZA–201302, and SKLF–KF–201203), the Natural Science Foundation of Jiangxi Province (20114BAB204019), the Program of Jiangxi Provincial Department of Science and Technology (20112BBF60010), and the Jiangxi Provincial Postgraduate Innovation Fund (YC2013-S049).
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