5-(Dimethylamino)naphthalene-1 -sulfonic Acid, a Fluorescent Probe of the Medium Chain Fatty Acid Binding Site of Serum Albumin

Michael C. Doody; Antonio M. Gotto; Louis C. Smith

doi:10.1021/bi00530a005

5-(Dimethylamino)naphthalene-1 -sulfonic Acid, a Fluorescent Probe of the Medium Chain Fatty Acid Binding Site of Serum Albumin

Michael C. Doody, Antonio M. Gotto, Louis C. Smith

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

Reversible binding of 5-(dimethylamino)-naphthalene-1-sulfonic acid (DNS) to human and bovine serum albumin has been monitored by changes in fluorescence intensity, wavelength maxima, and polarization. DNS has only one major binding site (k_a = 5 × 10⁶) and one minor site (k_a = 3 × 10⁵) on these proteins. The probe is competitively displaced from its high-affinity site by medium chain fatty acids and by N-acetyl-L-tryptophan. The binding site for DNS is highly hydrophobic and is considerably less polar than the hydrocarbon region of lipid bilayers. Resonance energy transfer indicates that the binding site is located 20.7 ± 2 Å from the single tryptophan residue of human serum albumin.

Original language	English (US)
Pages (from-to)	28-33
Number of pages	6
Journal	Biochemistry
Volume	21
Issue number	1
DOIs	https://doi.org/10.1021/bi00530a005
State	Published - Jan 1982

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Biochemistry

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title = "5-(Dimethylamino)naphthalene-1 -sulfonic Acid, a Fluorescent Probe of the Medium Chain Fatty Acid Binding Site of Serum Albumin",

abstract = "Reversible binding of 5-(dimethylamino)-naphthalene-1-sulfonic acid (DNS) to human and bovine serum albumin has been monitored by changes in fluorescence intensity, wavelength maxima, and polarization. DNS has only one major binding site (ka = 5 × 106) and one minor site (ka = 3 × 105) on these proteins. The probe is competitively displaced from its high-affinity site by medium chain fatty acids and by N-acetyl-L-tryptophan. The binding site for DNS is highly hydrophobic and is considerably less polar than the hydrocarbon region of lipid bilayers. Resonance energy transfer indicates that the binding site is located 20.7 ± 2 {\AA} from the single tryptophan residue of human serum albumin.",

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year = "1982",

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T1 - 5-(Dimethylamino)naphthalene-1 -sulfonic Acid, a Fluorescent Probe of the Medium Chain Fatty Acid Binding Site of Serum Albumin

AU - Doody, Michael C.

AU - Gotto, Antonio M.

AU - Smith, Louis C.

PY - 1982/1

Y1 - 1982/1

N2 - Reversible binding of 5-(dimethylamino)-naphthalene-1-sulfonic acid (DNS) to human and bovine serum albumin has been monitored by changes in fluorescence intensity, wavelength maxima, and polarization. DNS has only one major binding site (ka = 5 × 106) and one minor site (ka = 3 × 105) on these proteins. The probe is competitively displaced from its high-affinity site by medium chain fatty acids and by N-acetyl-L-tryptophan. The binding site for DNS is highly hydrophobic and is considerably less polar than the hydrocarbon region of lipid bilayers. Resonance energy transfer indicates that the binding site is located 20.7 ± 2 Å from the single tryptophan residue of human serum albumin.

AB - Reversible binding of 5-(dimethylamino)-naphthalene-1-sulfonic acid (DNS) to human and bovine serum albumin has been monitored by changes in fluorescence intensity, wavelength maxima, and polarization. DNS has only one major binding site (ka = 5 × 106) and one minor site (ka = 3 × 105) on these proteins. The probe is competitively displaced from its high-affinity site by medium chain fatty acids and by N-acetyl-L-tryptophan. The binding site for DNS is highly hydrophobic and is considerably less polar than the hydrocarbon region of lipid bilayers. Resonance energy transfer indicates that the binding site is located 20.7 ± 2 Å from the single tryptophan residue of human serum albumin.

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5-(Dimethylamino)naphthalene-1 -sulfonic Acid, a Fluorescent Probe of the Medium Chain Fatty Acid Binding Site of Serum Albumin

Abstract

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