{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang T"],"funding":["National Natural Science Foundation of China"],"pagination":["988"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8997858"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(7)"],"pubmed_abstract":["The present study aims to investigate the effects of ultrasound on the non-covalent interaction of β-lactoglobulin (β-LG) and luteolin (LUT) and to investigate the relationship between allergenicity and human intestinal microbiota. After treatment, the conformational structures of β-LG were changed, which reflected by the decrease in α-helix content, intrinsic fluorescence intensity and surface hydrophobicity, whereas the β-sheet content increased. Molecular docking studies revealed the non-covalent interaction of β-LG and LUT by hydrogen bond, van der Walls bond and hydrophobic bond. β-LG-LUT complex treated by ultrasound has a lower IgG/IgE binding ability and inhibits the allergic reaction of KU812 cells, depending on the changes in the conformational epitopes of β-LG. Meanwhile, the β-"],"journal":["Foods (Basel, Switzerland)"],"pubmed_title":["Ultrasound Improved the Non-Covalent Interaction of β-Lactoglobulin with Luteolin: Regulating Human Intestinal Microbiota and Conformational Epitopes Reduced Allergy Risks."],"pmcid":["PMC8997858"],"funding_grant_id":["31960457"],"pubmed_authors":["Liu J","Shao Y","Wang T","Chen W","Tu Z"],"additional_accession":[]},"is_claimable":false,"name":"Ultrasound Improved the Non-Covalent Interaction of β-Lactoglobulin with Luteolin: Regulating Human Intestinal Microbiota and Conformational Epitopes Reduced Allergy Risks.","description":"The present study aims to investigate the effects of ultrasound on the non-covalent interaction of β-lactoglobulin (β-LG) and luteolin (LUT) and to investigate the relationship between allergenicity and human intestinal microbiota. After treatment, the conformational structures of β-LG were changed, which reflected by the decrease in α-helix content, intrinsic fluorescence intensity and surface hydrophobicity, whereas the β-sheet content increased. Molecular docking studies revealed the non-covalent interaction of β-LG and LUT by hydrogen bond, van der Walls bond and hydrophobic bond. β-LG-LUT complex treated by ultrasound has a lower IgG/IgE binding ability and inhibits the allergic reaction of KU812 cells, depending on the changes in the conformational epitopes of β-LG. Meanwhile, the β-","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2025-04-26T13:05:42.337Z","creation":"2025-04-06T14:09:41.147Z"},"accession":"S-EPMC8997858","cross_references":{"pubmed":["35407075"],"doi":["10.3390/foods11070988"]}}