Title : The increased binding affinity of curcumin with human serum albumin in the presence of rutin and baicalin: A potential for drug delivery system.

Pub. Date : 2016 Feb 15

PMID : 26583522






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 The results showed that the fluorescence quenching of HSA by CU was a simultaneous static and dynamic quenching process, irrespective of the presence or absence of flavonoids. Flavonoids albumin Homo sapiens
2 The binding constants between CU and HSA in the absence and presence of rutin and baicalin were 2.268x10(5)M(-1), 3.062x10(5)M(-1), and 3.271x10(5)M(-1), indicating that the binding affinity was increased in the case of two flavonoids. Flavonoids albumin Homo sapiens
3 Combined with the fact that flavonoids and CU have the same binding site (site I), it can be concluded that they may simultaneously bind in different regions in site I, and formed a ternary complex of flavonoid-HSA-CU. Flavonoids albumin Homo sapiens
4 Combined with the fact that flavonoids and CU have the same binding site (site I), it can be concluded that they may simultaneously bind in different regions in site I, and formed a ternary complex of flavonoid-HSA-CU. Flavonoids albumin Homo sapiens
5 Meanwhile, the results of fluorescence quenching, CD and three-dimensional fluorescence spectra revealed that flavonoids further strengthened the microenvironmental and conformational changes of HSA induced by CU binding. Flavonoids albumin Homo sapiens