{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Khan MS"],"funding":["King Saud University"],"pagination":["26710-26720"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9037349"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(43)"],"pubmed_abstract":["Lactoferrin is a heme-binding multifunctional glycoprotein known for iron transportation in the blood and also contributes to innate immunity. In this study, the interaction of theaflavin monogallate, a polyphenolic component of black tea, with camel milk lactoferrin was studied using various biophysical and computational techniques. Fluorescence quenching at different temperatures suggests that theaflavin monogallate interacted with lactoferrin by forming a non-fluorescent complex, <i>i.e.</i>, static quenching. Theaflavin monogallate shows a significant affinity towards lactoferrin with a binding constant of ∼10<sup>4</sup>-10<sup>5</sup> M<sup>-1</sup> at different temperatures. ANS binding shows that the binding of polyphenol resulted in the burial of hydrophobic domains of lactoferrin"],"journal":["RSC advances"],"pubmed_title":["Elucidation of molecular interactions of theaflavin monogallate with camel milk lactoferrin: detailed spectroscopic and dynamic simulation studies."],"pmcid":["PMC9037349"],"funding_grant_id":["RSP-2021/352"],"pubmed_authors":["Alsalme AM","Khan RA","Rehman MT","Husain FM","Altwaijry N","Ismael MA","Khan MS","Alokail MS","AlAjmi MF"],"additional_accession":[]},"is_claimable":false,"name":"Elucidation of molecular interactions of theaflavin monogallate with camel milk lactoferrin: detailed spectroscopic and dynamic simulation studies.","description":"Lactoferrin is a heme-binding multifunctional glycoprotein known for iron transportation in the blood and also contributes to innate immunity. In this study, the interaction of theaflavin monogallate, a polyphenolic component of black tea, with camel milk lactoferrin was studied using various biophysical and computational techniques. Fluorescence quenching at different temperatures suggests that theaflavin monogallate interacted with lactoferrin by forming a non-fluorescent complex, <i>i.e.</i>, static quenching. Theaflavin monogallate shows a significant affinity towards lactoferrin with a binding constant of ∼10<sup>4</sup>-10<sup>5</sup> M<sup>-1</sup> at different temperatures. ANS binding shows that the binding of polyphenol resulted in the burial of hydrophobic domains of lactoferrin","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Aug","modification":"2026-05-31T18:50:01.468Z","creation":"2025-04-05T22:20:24.981Z"},"accession":"S-EPMC9037349","cross_references":{"pubmed":["35479994"],"doi":["10.1039/d1ra03256a"]}}