2023
DOI: 10.1039/d3ra00375b
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Insight into the interaction between tannin acid and bovine serum albumin from a spectroscopic and molecular docking perspective

Abstract: Based on non-covalent bonds, TA could change the secondary structure change of BSA to a certain extent, and improve its thermostability.

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Cited by 5 publications
(2 citation statements)
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References 41 publications
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“…TA only benefits the body when its concentration in food is not too high. TA contains active hydroxyl and carboxyl groups that can form complexes with proteins, polysaccharides, alkaloids, and nucleic acids [29,100]. These properties can impede the digestion and absorption of nutrients.…”
Section: Discussionmentioning
confidence: 99%
“…TA only benefits the body when its concentration in food is not too high. TA contains active hydroxyl and carboxyl groups that can form complexes with proteins, polysaccharides, alkaloids, and nucleic acids [29,100]. These properties can impede the digestion and absorption of nutrients.…”
Section: Discussionmentioning
confidence: 99%
“…Bovine serum albumin (BSA) was extensively investigated as a model globular protein, being one of the most important transporters for endogenous and exogenous molecules in the blood [26,27]. This globular macromolecule presents a predominantly α-helix structure (67%) [28] composed of around 583 amino acid residues.…”
Section: Introductionmentioning
confidence: 99%