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Substitution at the C-3 Position of Catechins Has an Influence on the Binding Affinities against Serum Albumin
- Source :
- Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry, Molecules; Volume 22; Issue 2; Pages: 314, Molecules, Vol 22, Iss 2, p 314 (2017)
- Publication Year :
- 2017
- Publisher :
- MDPI, 2017.
-
Abstract
- It is known that catechins interact with the tryptophan (Trp) residue at the drug-binding site of serum albumin. In this study, we used catechin derivatives to investigate which position of the catechin structure strongly influences the binding affinity against bovine serum albumin (BSA) and human serum albumin (HSA). A docking simulation showed that (−)-epigallocatechin gallate (EGCg) interacted with both Trp residues of BSA (one at drug-binding site I and the other on the molecular surface), mainly by π–π stacking. Fluorescence analysis showed that EGCg and substituted EGCg caused a red shift of the peak wavelength of Trp similarly to warfarin (a drug-binding site I-specific compound), while 3-O-acyl-catechins caused a blue shift. To evaluate the binding affinities, the quenching constants were determined by the Stern–Volmer equation. A gallate ester at the C-3 position increased the quenching constants of the catechins. Against BSA, acyl substitution increased the quenching constant proportionally to the carbon chain lengths of the acyl group, whereas methyl substitution decreased the quenching constant. Against HSA, neither acyl nor methyl substitution affected the quenching constant. In conclusion, substitution at the C-3 position of catechins has an important influence on the binding affinity against serum albumin.
- Subjects :
- 0301 basic medicine
Models, Molecular
Stereochemistry
serum albumin
Serum albumin
Molecular Conformation
Pharmaceutical Science
interaction
01 natural sciences
Article
Catechin
Analytical Chemistry
lcsh:QD241-441
03 medical and health sciences
chemistry.chemical_compound
fluorescence analysis
lcsh:Organic chemistry
Drug Discovery
medicine
Animals
Humans
Physical and Theoretical Chemistry
Bovine serum albumin
catechin
docking study
biology
010405 organic chemistry
Chemistry
Organic Chemistry
Nucleophilic acyl substitution
Tryptophan
Serum Albumin, Bovine
Gallate
Human serum albumin
0104 chemical sciences
030104 developmental biology
Chemistry (miscellaneous)
Docking (molecular)
biology.protein
Molecular Medicine
Cattle
Acyl group
medicine.drug
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 14203049
- Volume :
- 22
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Molecules
- Accession number :
- edsair.doi.dedup.....599ad981fb654299bb01b66678c1a3f2