Imaging human serum albumin behavior in process of PVOCs transportation in vivo: Spectroscopy analysis insight

• Published in: Food chemistry 2022-12, Vol.396, p.133692-133692, Article 133692
• Main Authors: Geng, Zhaoming, Zhou, Qingteng, Guo, Ming, Yao, Yecen, Tian, Luwei, Lin, Haiping
• Format: Article
• Language: English
• Subjects: Fingerprint pattern; HSA; Molecular modeling; Pomelo volatile organic compounds
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2022.133692

[Display omitted] •21 VOCs of 9 pomelos were obtained and 3 key pomelos VOCs were screened out.•Binding of VOCs with HSA changes the HSA secondary structure was found.•Fingerprints for HSA binding with pomelo VOCs were established.•Spectral and analog design confirm VOCs with HSA showing high affinity binding. Pomelo volatile organic compounds (PVOCs) are used as food additives to provide unique flavors, thus, and the possible effects of VOC binding to albumin should be considered. Headspace solid-phase microextraction with gas chromatography-mass spectrometry was used to fingerprints adsorption of PVOCs on human serum albumin (HSA). Spectral data and molecular modeling were used to establish a binding model between PVOCs and HSA. Twenty-one common components were identified, and dipentene, linalylacetate, and nootkatone were identified as characteristic components. Thermodynamic calculations showed that dipentene and linalylacetate bound to HSA via van der Waals forces and hydrophobic interactions, whereas nootkatone bound to HSA via van der Waals forces alone. Molecular modeling showed that the volatile components were all bound to the hydrophobic pocket of HSA site I. Our results provide a useful basis for quality evaluation of pomelo and explain the mechanism of interaction between PVOCs and HSA.