Study On The Interaction Of Several Important Active Components In Edible And Medicinal Fungi With Human Serum Albumin

The chemical components currently isolated and identified from edible and medicinal fungi are mainly terpenoids(triterpenes,diterpenes and sesquiterpenes),steroids,alkaloids,sphingolipids,pigments,polysaccharides,other types of components and so on.The common methods for quality evaluation include thin layer chromatography,ultraviolet spectrophotometry,titration,high performance liquid chromatography,fingerprint analysis and so on.The quality evaluation was carried out by measuring the content of the main component,the active component or the characteristic component.The quality evaluation has not systematically studied the transmission mechanism of the active component in the human body.The interaction mechanism of several important active components in edible and medicinal fungi with human serum albumin were systematically studied by fluorescence spectroscopy,synchronous fluorescence spectroscopy,three-dimensional fluorescence spectroscopy,UV-visible absorption spectroscopy and molecular docking approach for the purpose of revealing the transmission mechanism of those active components in the human body.These results laid the foundation for quality evaluation.(1)Under simulated physiological conditions,the mechanism and conformational changes were systematically investigated for the interaction between ergocalciferol of Lentinula edodes and human serum albumin.The results indicated that ergocalciferol quenched the endogenous fluorescence of human serum albumin through static quenching mechanism.As for binding ergocalciferol and human serum albumin at 288 K was favorable while at higher temperature was unfavorable.The hydrophobic interactions,van der Waals force and hydrogen bonding were the primary forces during the binding process.The site I was the major binding site for the interaction between ergocalciferol and human serum albumin.The energy transfer could occur during the binding process and the binding distance was 3.46 nm.The structure and microenvironment of human serum albumin were slightly changed during the binding process.These results not only revealed the transmission mechanism of ergocalciferol in the human body,but also laid the foundation for the quality evaluation of Lentinula edodes.(2)Under simulated physiological conditions,the mechanism and conformational changes were systematically investigated for the interaction between dehydroeburicoic acid of Fomitopsis pinicola and human serum albumin.The results indicated dehydroeburicoic acid quenched the endogenous fluorescence of human serum albumin through the combination of static and dynamic quenching mechanism.The hydrogen bonding,hydrophobic force and van der Waals force were major acting forces during the binding process.The site II was the major binding site during the binding process.The energy transfer could occur during the binding process and the binding distance was 3.29 nm.The binding process slightly changed the conformation and microenvironment of human serum albumin.The dehydroeburicoic acid molecule entered the hydrophobic cleft of human serum albumin and formed the hydrogen bonding with Glu-492 and Lys-545.These results not only revealed the transmission mechanism of dehydroeburicoic acid in the human body,but also laid the foundation for the quality evaluation of Fomitopsis pinicola.(3)Under simulated physiological conditions,the mechanism and conformational changes were systematically investigated for the interaction between verbascoside of Pleurotus ostreatus and human serum albumin.The results indicated the verbascoside quenched the endogenous fluorescence of human serum albumin through the combination of static and dynamic quenching mechanism.The hydrogen bonding,hydrophobic force and van der Waals force were major acting forces during the binding process.Verbascoside bound to human serum albumin at site II(subdomain IIIA).The interaction between verbascoside and human serum albumin changed the polarity and microenvironment around tyrosine residues.The dehydroeburicoic acid molecule entered the hydrophobic cleft of human serum albumin and formed the hydrogen bonding with Lys-413 and Lys-541.These results not only revealed the transmission mechanism of verbascoside in the human body,but also laid the foundation for the quality evaluation of Pleurotus ostreatus.(4)Under simulated physiological conditions,the mechanism and conformational changes were systematically investigated for the interaction between ergosterol peroxide of Leucocalocybe mongolica and human serum albumin.The results indicated the ergosterol peroxide quenched the endogenous fluorescence of human serum albumin through static quenching mechanism.The energy transfer could occur during the binding process and the binding distance was 3.37 nm.The hydrophobic force were major acting forces during the binding process.The stable ergosterol peroxide-human serum albumin complex was formed during the binding process,which facilitated the transmission of ergosterol peroxide in the human body.The site I was the major binding site during the binding process.The binding process slightly changed the conformation and microenvironment of human serum albumin.These results not only revealed the transmission mechanism of ergosterol peroxide in the human body,but also laid the foundation for the quality evaluation of Leucocalocybe mongolica.(5)The molecular mechanism was studied by molecular docking approach for the interaction between photosensitive toxic components of Bulgaria inquinans and immunoglobulin E.The results indicated dibutyl phthalate and diisobutyl phthalate bound immunoglobulin E at two different binding sites.The hydrogen bonding and hydrophobic interaction were main forces for the interaction of dibutyl phthalate and diisobutyl phthalate with immunoglobulin E.The ester groups of the dibutyl phthalate and diisobutyl phthalate molecules were important groups in their allergic reactions.Val-476 of immunoglobulin E was an important amino acid residue during the binding process.The binding ability of diisobutyl phthalate and immunoglobulin E was stronger than that of dibutyl phthalate.These results are important for revealing the photosensitivity mechanism and safety evaluation of Bulgaria inquinans.Under simulated physiological conditions,the mechanism and conformational changes were systematically investigated for the interaction of several important active components in edible and medicinal fungi with human serum albumin.These help to understand coordination nature of the interaction between these active components and human serum albumin at the molecular level.These facilitate the modification,design and development of these active components.It is significant to deeply understand the pharmacodynamics and pharmacokinetics properties of these active components.This will lay the foundation for the quality evaluation of these kinds of mushroom crops.