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.
| Language | English |
|---|---|
| Article number | 314 |
| Journal | Molecules |
| Volume | 22 |
| Issue number | 2 |
| DOIs | |
| State | Published - 2017 Feb 1 |
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Keywords
- Catechin
- Docking study
- Fluorescence analysis
- Interaction
- Serum albumin
ASJC Scopus subject areas
- Medicine(all)
- Organic Chemistry
Cite this
Substitution at the C-3 position of catechins has an influence on the binding affinities against serum albumin. / Ikeda, Masaki; Ueda-Wakagi, Manabu; Hayashibara, Kaori; Kitano, Rei; Kawase, Masaya; Kaihatsu, Kunihiro; Kato, Nobuo; Suhara, Yoshitomo; Osakabe, Naomi; Ashida, Hitoshi.
In: Molecules, Vol. 22, No. 2, 314, 01.02.2017.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Substitution at the C-3 position of catechins has an influence on the binding affinities against serum albumin
AU - Ikeda,Masaki
AU - Ueda-Wakagi,Manabu
AU - Hayashibara,Kaori
AU - Kitano,Rei
AU - Kawase,Masaya
AU - Kaihatsu,Kunihiro
AU - Kato,Nobuo
AU - Suhara,Yoshitomo
AU - Osakabe,Naomi
AU - Ashida,Hitoshi
PY - 2017/2/1
Y1 - 2017/2/1
N2 - 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.
AB - 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.
KW - Catechin
KW - Docking study
KW - Fluorescence analysis
KW - Interaction
KW - Serum albumin
UR - http://www.scopus.com/inward/record.url?scp=85013226672&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85013226672&partnerID=8YFLogxK
U2 - 10.3390/molecules22020314
DO - 10.3390/molecules22020314
M3 - Article
VL - 22
JO - Molecules
T2 - Molecules
JF - Molecules
SN - 1420-3049
IS - 2
M1 - 314
ER -