Molecular basis of the Cotton effects induced by the binding of curcumin to human serum albumin

F. Zsila, Zsolt Bikádi, M. Simonyi

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

Curcumin binding to human serum albumin (HSA) has been found recently to induce bisignate CD curves due to intramolecular exciton coupling between the two feruloyl chromophoric parts. The present study reports further results on this interaction. UV-vis and chiroptical properties of HSA-bound curcumin were analyzed in detail by comparison with bilirubin-albumin complexes. Data obtained by UV-vis and fluorescence spectroscopy, CD displacement experiments and molecular modelling methods suggested the primary binding site of curcumin to be located in site I of HSA. Since acid-base dissociation of the polyphenol type curcumin molecule plays a fundamental role in albumin binding, light absorption spectra of curcumin and half-curcumin (dehydrozingerone) were studied in ethanol and in water at different pH values. It is established that the phenolic OH group of curcumin is the most acidic and that its dissociation is responsible for both the large red-shift of the main absorption band and the binding of curcumin to HSA in a right-handed chiral conformation. Additionally, it is demonstrated that pH dependent induced CD spectra can be utilized to determine the acid-base dissociation constant; from chiroptical data the first pKa value of curcumin was calculated (8.28).

Original languageEnglish
Pages (from-to)2433-2444
Number of pages12
JournalTetrahedron Asymmetry
Volume14
Issue number16
DOIs
Publication statusPublished - Aug 15 2003

Fingerprint

Curcumin
cotton
albumins
Serum Albumin
serums
Cotton
Absorption spectra
Molecular modeling
Acids
Fluorescence spectroscopy
Binding sites
dissociation
Ultraviolet spectroscopy
Excitons
Light absorption
Conformations
Ethanol
absorption spectra
acids
Molecules

ASJC Scopus subject areas

  • Inorganic Chemistry
  • Organic Chemistry
  • Materials Chemistry
  • Drug Discovery

Cite this

Molecular basis of the Cotton effects induced by the binding of curcumin to human serum albumin. / Zsila, F.; Bikádi, Zsolt; Simonyi, M.

In: Tetrahedron Asymmetry, Vol. 14, No. 16, 15.08.2003, p. 2433-2444.

Research output: Contribution to journalArticle

@article{67c7f40c74e844b0af0122ec84e19a57,
title = "Molecular basis of the Cotton effects induced by the binding of curcumin to human serum albumin",
abstract = "Curcumin binding to human serum albumin (HSA) has been found recently to induce bisignate CD curves due to intramolecular exciton coupling between the two feruloyl chromophoric parts. The present study reports further results on this interaction. UV-vis and chiroptical properties of HSA-bound curcumin were analyzed in detail by comparison with bilirubin-albumin complexes. Data obtained by UV-vis and fluorescence spectroscopy, CD displacement experiments and molecular modelling methods suggested the primary binding site of curcumin to be located in site I of HSA. Since acid-base dissociation of the polyphenol type curcumin molecule plays a fundamental role in albumin binding, light absorption spectra of curcumin and half-curcumin (dehydrozingerone) were studied in ethanol and in water at different pH values. It is established that the phenolic OH group of curcumin is the most acidic and that its dissociation is responsible for both the large red-shift of the main absorption band and the binding of curcumin to HSA in a right-handed chiral conformation. Additionally, it is demonstrated that pH dependent induced CD spectra can be utilized to determine the acid-base dissociation constant; from chiroptical data the first pKa value of curcumin was calculated (8.28).",
author = "F. Zsila and Zsolt Bik{\'a}di and M. Simonyi",
year = "2003",
month = "8",
day = "15",
doi = "10.1016/S0957-4166(03)00486-5",
language = "English",
volume = "14",
pages = "2433--2444",
journal = "Tetrahedron Asymmetry",
issn = "0957-4166",
publisher = "Elsevier Limited",
number = "16",

}

TY - JOUR

T1 - Molecular basis of the Cotton effects induced by the binding of curcumin to human serum albumin

AU - Zsila, F.

AU - Bikádi, Zsolt

AU - Simonyi, M.

PY - 2003/8/15

Y1 - 2003/8/15

N2 - Curcumin binding to human serum albumin (HSA) has been found recently to induce bisignate CD curves due to intramolecular exciton coupling between the two feruloyl chromophoric parts. The present study reports further results on this interaction. UV-vis and chiroptical properties of HSA-bound curcumin were analyzed in detail by comparison with bilirubin-albumin complexes. Data obtained by UV-vis and fluorescence spectroscopy, CD displacement experiments and molecular modelling methods suggested the primary binding site of curcumin to be located in site I of HSA. Since acid-base dissociation of the polyphenol type curcumin molecule plays a fundamental role in albumin binding, light absorption spectra of curcumin and half-curcumin (dehydrozingerone) were studied in ethanol and in water at different pH values. It is established that the phenolic OH group of curcumin is the most acidic and that its dissociation is responsible for both the large red-shift of the main absorption band and the binding of curcumin to HSA in a right-handed chiral conformation. Additionally, it is demonstrated that pH dependent induced CD spectra can be utilized to determine the acid-base dissociation constant; from chiroptical data the first pKa value of curcumin was calculated (8.28).

AB - Curcumin binding to human serum albumin (HSA) has been found recently to induce bisignate CD curves due to intramolecular exciton coupling between the two feruloyl chromophoric parts. The present study reports further results on this interaction. UV-vis and chiroptical properties of HSA-bound curcumin were analyzed in detail by comparison with bilirubin-albumin complexes. Data obtained by UV-vis and fluorescence spectroscopy, CD displacement experiments and molecular modelling methods suggested the primary binding site of curcumin to be located in site I of HSA. Since acid-base dissociation of the polyphenol type curcumin molecule plays a fundamental role in albumin binding, light absorption spectra of curcumin and half-curcumin (dehydrozingerone) were studied in ethanol and in water at different pH values. It is established that the phenolic OH group of curcumin is the most acidic and that its dissociation is responsible for both the large red-shift of the main absorption band and the binding of curcumin to HSA in a right-handed chiral conformation. Additionally, it is demonstrated that pH dependent induced CD spectra can be utilized to determine the acid-base dissociation constant; from chiroptical data the first pKa value of curcumin was calculated (8.28).

UR - http://www.scopus.com/inward/record.url?scp=0041562528&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0041562528&partnerID=8YFLogxK

U2 - 10.1016/S0957-4166(03)00486-5

DO - 10.1016/S0957-4166(03)00486-5

M3 - Article

VL - 14

SP - 2433

EP - 2444

JO - Tetrahedron Asymmetry

JF - Tetrahedron Asymmetry

SN - 0957-4166

IS - 16

ER -