Conjugated polyene fatty acids as fluorescent probes

Binding to bovine serum albumin

Larry A. Sklar, Bruce S Hudson, Robert D. Simoni

Research output: Contribution to journalArticle

347 Citations (Scopus)

Abstract

The binding of the conjugated polyene fatty acids, cis-parinaric acid (9,11,13,15-cis,trans,trans,cis-octadecatetraenoic acid) and cis-eleostearic acid (9,11,13-cis-trans,trans-octadecatrienoic acid), to bovine serum albumin has been studied by using absorption and fluorescence properties of the polyene chromophores. These studies demonstrate the utility of polyene fatty acids as probes of lipid-protein interactions. Shifts in the absorption spectrum, enhancement of parinaric acid fluorescence, induced circular dichroism in the polyene chromophore, and energy transfer between the tryptophan residues and the bound chromophores all provide information about the binding of these fatty acids to albumin. Strong reversible binding of parinaric acid and eleostearic acid to bovine serum albumin is observed. Fluorescence and absorption measurements demonstrate that there are binding sites for approximately five fatty acid molecules with binding conslants ∼106 to 108 M-1, similar to previous results for oleic acid. An induced circular dichroism arises when the polyene is bound to approximately four of these tightest binding sites. This circular dichroism is complex when more than one parinaric acid molecule is bound to the protein and is attributed to excitonic ligand-ligand interactions. Fluorescence quenching of the albumin tryptophan residues by parinaric acid is more efficient than quenching by eleostearic acid, consistent with expectations for singlet-singlet Förster transfer. The availability of two homologous polyene fatty acids with very different spectral overlap integrals with tryptophan enhances the reliability of intramolecular distance determinations by the energy transfer technique. A procedure is given for the decomposition of the total energy transfer efficiency into the contributions for each of the two tryptophan donors.

Original languageEnglish (US)
Pages (from-to)5100-5108
Number of pages9
JournalBiochemistry
Volume16
Issue number23
StatePublished - 1977
Externally publishedYes

Fingerprint

Polyenes
Bovine Serum Albumin
Fluorescent Dyes
NSC 153174
Fatty Acids
Tryptophan
Energy Transfer
Chromophores
Circular Dichroism
Fluorescence
Energy transfer
Albumins
Quenching
Binding Sites
Ligands
Molecules
Oleic Acid
parinaric acid
Absorption spectra
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Sklar, L. A., Hudson, B. S., & Simoni, R. D. (1977). Conjugated polyene fatty acids as fluorescent probes: Binding to bovine serum albumin. Biochemistry, 16(23), 5100-5108.

Conjugated polyene fatty acids as fluorescent probes : Binding to bovine serum albumin. / Sklar, Larry A.; Hudson, Bruce S; Simoni, Robert D.

In: Biochemistry, Vol. 16, No. 23, 1977, p. 5100-5108.

Research output: Contribution to journalArticle

Sklar, LA, Hudson, BS & Simoni, RD 1977, 'Conjugated polyene fatty acids as fluorescent probes: Binding to bovine serum albumin', Biochemistry, vol. 16, no. 23, pp. 5100-5108.
Sklar, Larry A. ; Hudson, Bruce S ; Simoni, Robert D. / Conjugated polyene fatty acids as fluorescent probes : Binding to bovine serum albumin. In: Biochemistry. 1977 ; Vol. 16, No. 23. pp. 5100-5108.
@article{9823b5d7b75d49c3a77f4bbe6b59b30b,
title = "Conjugated polyene fatty acids as fluorescent probes: Binding to bovine serum albumin",
abstract = "The binding of the conjugated polyene fatty acids, cis-parinaric acid (9,11,13,15-cis,trans,trans,cis-octadecatetraenoic acid) and cis-eleostearic acid (9,11,13-cis-trans,trans-octadecatrienoic acid), to bovine serum albumin has been studied by using absorption and fluorescence properties of the polyene chromophores. These studies demonstrate the utility of polyene fatty acids as probes of lipid-protein interactions. Shifts in the absorption spectrum, enhancement of parinaric acid fluorescence, induced circular dichroism in the polyene chromophore, and energy transfer between the tryptophan residues and the bound chromophores all provide information about the binding of these fatty acids to albumin. Strong reversible binding of parinaric acid and eleostearic acid to bovine serum albumin is observed. Fluorescence and absorption measurements demonstrate that there are binding sites for approximately five fatty acid molecules with binding conslants ∼106 to 108 M-1, similar to previous results for oleic acid. An induced circular dichroism arises when the polyene is bound to approximately four of these tightest binding sites. This circular dichroism is complex when more than one parinaric acid molecule is bound to the protein and is attributed to excitonic ligand-ligand interactions. Fluorescence quenching of the albumin tryptophan residues by parinaric acid is more efficient than quenching by eleostearic acid, consistent with expectations for singlet-singlet F{\"o}rster transfer. The availability of two homologous polyene fatty acids with very different spectral overlap integrals with tryptophan enhances the reliability of intramolecular distance determinations by the energy transfer technique. A procedure is given for the decomposition of the total energy transfer efficiency into the contributions for each of the two tryptophan donors.",
author = "Sklar, {Larry A.} and Hudson, {Bruce S} and Simoni, {Robert D.}",
year = "1977",
language = "English (US)",
volume = "16",
pages = "5100--5108",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "23",

}

TY - JOUR

T1 - Conjugated polyene fatty acids as fluorescent probes

T2 - Binding to bovine serum albumin

AU - Sklar, Larry A.

AU - Hudson, Bruce S

AU - Simoni, Robert D.

PY - 1977

Y1 - 1977

N2 - The binding of the conjugated polyene fatty acids, cis-parinaric acid (9,11,13,15-cis,trans,trans,cis-octadecatetraenoic acid) and cis-eleostearic acid (9,11,13-cis-trans,trans-octadecatrienoic acid), to bovine serum albumin has been studied by using absorption and fluorescence properties of the polyene chromophores. These studies demonstrate the utility of polyene fatty acids as probes of lipid-protein interactions. Shifts in the absorption spectrum, enhancement of parinaric acid fluorescence, induced circular dichroism in the polyene chromophore, and energy transfer between the tryptophan residues and the bound chromophores all provide information about the binding of these fatty acids to albumin. Strong reversible binding of parinaric acid and eleostearic acid to bovine serum albumin is observed. Fluorescence and absorption measurements demonstrate that there are binding sites for approximately five fatty acid molecules with binding conslants ∼106 to 108 M-1, similar to previous results for oleic acid. An induced circular dichroism arises when the polyene is bound to approximately four of these tightest binding sites. This circular dichroism is complex when more than one parinaric acid molecule is bound to the protein and is attributed to excitonic ligand-ligand interactions. Fluorescence quenching of the albumin tryptophan residues by parinaric acid is more efficient than quenching by eleostearic acid, consistent with expectations for singlet-singlet Förster transfer. The availability of two homologous polyene fatty acids with very different spectral overlap integrals with tryptophan enhances the reliability of intramolecular distance determinations by the energy transfer technique. A procedure is given for the decomposition of the total energy transfer efficiency into the contributions for each of the two tryptophan donors.

AB - The binding of the conjugated polyene fatty acids, cis-parinaric acid (9,11,13,15-cis,trans,trans,cis-octadecatetraenoic acid) and cis-eleostearic acid (9,11,13-cis-trans,trans-octadecatrienoic acid), to bovine serum albumin has been studied by using absorption and fluorescence properties of the polyene chromophores. These studies demonstrate the utility of polyene fatty acids as probes of lipid-protein interactions. Shifts in the absorption spectrum, enhancement of parinaric acid fluorescence, induced circular dichroism in the polyene chromophore, and energy transfer between the tryptophan residues and the bound chromophores all provide information about the binding of these fatty acids to albumin. Strong reversible binding of parinaric acid and eleostearic acid to bovine serum albumin is observed. Fluorescence and absorption measurements demonstrate that there are binding sites for approximately five fatty acid molecules with binding conslants ∼106 to 108 M-1, similar to previous results for oleic acid. An induced circular dichroism arises when the polyene is bound to approximately four of these tightest binding sites. This circular dichroism is complex when more than one parinaric acid molecule is bound to the protein and is attributed to excitonic ligand-ligand interactions. Fluorescence quenching of the albumin tryptophan residues by parinaric acid is more efficient than quenching by eleostearic acid, consistent with expectations for singlet-singlet Förster transfer. The availability of two homologous polyene fatty acids with very different spectral overlap integrals with tryptophan enhances the reliability of intramolecular distance determinations by the energy transfer technique. A procedure is given for the decomposition of the total energy transfer efficiency into the contributions for each of the two tryptophan donors.

UR - http://www.scopus.com/inward/record.url?scp=0017661379&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017661379&partnerID=8YFLogxK

M3 - Article

VL - 16

SP - 5100

EP - 5108

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 23

ER -