{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lei S"],"funding":["the National Key R&D Program of China","the Priority Academic Program Development of Jiangsu Higher Education Institutions","Key Technology R&D Program of Jiangsu Province"],"pagination":["3421-3432"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5629150"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["54(11)"],"pubmed_abstract":["In this study, theaflavins (TF1, TF2A, TF2B and TF3) were prepared from black tea and their interaction with bovine serum albumin (BSA) was explored by fluorescence and CD spectroscopy. The results showed that the structures of theaflavins exhibited significant effects on the binding/quenching process, and the binding affinity increased with the increase of molecular weight of theaflavins and the presence of galloyl moiety. The quenching effects showed a sequence as TF3 > TF2A > TF2B > TF1, demonstrating the important role of the galloyl moiety on the C-3 position of theaflavins. CD spectra indicated that TF3 in high concentration could change the skeleton structure of BSA and induce the unfolding of BSA secondary structure. The present results provide a new perspective for better understa"],"journal":["Journal of food science and technology"],"pubmed_title":["Characterization of molecular structures of theaflavins and the interactions with bovine serum albumin."],"pmcid":["PMC5629150"],"funding_grant_id":["PAPD","BE2013313","2017YFD0400800"],"pubmed_authors":["Riaz A","Xu D","Zeng X","Lei S","Saeeduddin M"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of molecular structures of theaflavins and the interactions with bovine serum albumin.","description":"In this study, theaflavins (TF1, TF2A, TF2B and TF3) were prepared from black tea and their interaction with bovine serum albumin (BSA) was explored by fluorescence and CD spectroscopy. The results showed that the structures of theaflavins exhibited significant effects on the binding/quenching process, and the binding affinity increased with the increase of molecular weight of theaflavins and the presence of galloyl moiety. The quenching effects showed a sequence as TF3 > TF2A > TF2B > TF1, demonstrating the important role of the galloyl moiety on the C-3 position of theaflavins. CD spectra indicated that TF3 in high concentration could change the skeleton structure of BSA and induce the unfolding of BSA secondary structure. The present results provide a new perspective for better understa","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Oct","modification":"2025-04-26T01:22:48.015Z","creation":"2019-03-26T23:57:56Z"},"accession":"S-EPMC5629150","cross_references":{"pubmed":["29051637"],"doi":["10.1007/s13197-017-2791-5"]}}