Plasma protein binding of dietary polyphenols to human serum albumin: A high performance affinity chromatography approach
Autor: | Pradeep K. Sengupta, Jianbo Xiao, Xiaojuan Liu, Hui Cao, Nataša Poklar Ulrih |
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Rok vydání: | 2018 |
Předmět: |
Stereochemistry
Serum albumin Serum Albumin Human Plasma protein binding 01 natural sciences Chromatography Affinity Analytical Chemistry Hydroxylation chemistry.chemical_compound Structure-Activity Relationship 0404 agricultural biotechnology Blood serum Affinity chromatography medicine Humans Flavonoids biology 010401 analytical chemistry Polyphenols 04 agricultural and veterinary sciences General Medicine Blood Proteins Human serum albumin 040401 food science Blood proteins 0104 chemical sciences chemistry biology.protein Flavanone Food Science medicine.drug Protein Binding |
Zdroj: | Food chemistry. 270 |
ISSN: | 1873-7072 |
Popis: | Herein, the protein binding rates of structurally different flavonoids to human serum albumin (HSA) were elucidated by applying the high performance affinity chromatography (HPAC). The flavonoids with hydroxyl groups on ring A showed a higher protein binding rate compared with those that there was no hydroxyl on ring A. However, the hydroxylation of ring B lowered the protein binding rate. It was also found that an additional methoxy group in flavone ring A would decrease the protein binding rate. Nevertheless, the methoxy group in flavanone ring A (position 6) and isoflavone ring B (position 4') increased the protein binding rate. Methoxy group at other positions of flavonoids slightly enhanced or no significantly affected the binding rates on human serum albumin. Hydrogenation of C2C3 double bond of flavonoids decreased the protein binding rate and had the same effect as glycosylation which decrease the protein binding rate by 5%-25%. |
Databáze: | OpenAIRE |
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