Complementary Fluorescence and Phosphorescence Study of the Interaction of Brompheniramine with Human Serum Albumin

S. Tardioli, I. mr. Lammers, J.H. Hooijschuur, F. Ariese, G. van der Zwan, C. Gooijer

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Binding of the antihistamine drug brompheniramine (BPA) to human serum albumin (HSA) is studied by measuring quenching of the fluorescence and room temperature phosphorescence (RTP) of tryptophan. The modified Stern-Volmer equation was used to derive association constants and accessible fractions from the steady-state fluorescence data. Decay associated spectra (DAS) revealed three tryptophan fluorescence lifetimes, indicating the presence of three HSA conformations. BPA causes mainly static quenching of the long-living, solvent-exposed conformer. RTP spectra and lifetimes, recorded under deoxygenated conditions in the presence of 0.2 M KI, provided additional kinetic information about the HSA-BPA interactions. Fluorescence DAS that were also recorded in the presence of 0.2 M KI revealed that the solvent-exposed conformer is the major contributor to the RTP signal. The phosphorescence quenching is mostly dynamic at pH 7 and mostly static at pH 9, presumably related to the protonation state of the alkylamino chain of BPA. This provides direct insight into the binding mode of the antihistamine drug, as well as kinetic information at both the nanosecond and the millisecond time scales. © 2012 American Chemical Society.
Original languageEnglish
Pages (from-to)7033-7039
Number of pages7
JournalJournal of Physical Chemistry B
Volume116
Issue number24
DOIs
Publication statusPublished - 2012

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Brompheniramine
Phosphorescence
phosphorescence
albumins
Serum Albumin
serums
Fluorescence
Quenching
fluorescence
Histamine Antagonists
tryptophan
quenching
Tryptophan
drugs
room temperature
interactions
life (durability)
Kinetics
Protonation
kinetics

Cite this

@article{d2756a63b89d4118a26f8b753567195e,
title = "Complementary Fluorescence and Phosphorescence Study of the Interaction of Brompheniramine with Human Serum Albumin",
abstract = "Binding of the antihistamine drug brompheniramine (BPA) to human serum albumin (HSA) is studied by measuring quenching of the fluorescence and room temperature phosphorescence (RTP) of tryptophan. The modified Stern-Volmer equation was used to derive association constants and accessible fractions from the steady-state fluorescence data. Decay associated spectra (DAS) revealed three tryptophan fluorescence lifetimes, indicating the presence of three HSA conformations. BPA causes mainly static quenching of the long-living, solvent-exposed conformer. RTP spectra and lifetimes, recorded under deoxygenated conditions in the presence of 0.2 M KI, provided additional kinetic information about the HSA-BPA interactions. Fluorescence DAS that were also recorded in the presence of 0.2 M KI revealed that the solvent-exposed conformer is the major contributor to the RTP signal. The phosphorescence quenching is mostly dynamic at pH 7 and mostly static at pH 9, presumably related to the protonation state of the alkylamino chain of BPA. This provides direct insight into the binding mode of the antihistamine drug, as well as kinetic information at both the nanosecond and the millisecond time scales. {\circledC} 2012 American Chemical Society.",
author = "S. Tardioli and {mr. Lammers}, I. and J.H. Hooijschuur and F. Ariese and {van der Zwan}, G. and C. Gooijer",
year = "2012",
doi = "10.1021/jp300055c",
language = "English",
volume = "116",
pages = "7033--7039",
journal = "Journal of Physical Chemistry B",
issn = "1520-6106",
publisher = "American Chemical Society",
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}

Complementary Fluorescence and Phosphorescence Study of the Interaction of Brompheniramine with Human Serum Albumin. / Tardioli, S.; mr. Lammers, I.; Hooijschuur, J.H.; Ariese, F.; van der Zwan, G.; Gooijer, C.

In: Journal of Physical Chemistry B, Vol. 116, No. 24, 2012, p. 7033-7039.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Complementary Fluorescence and Phosphorescence Study of the Interaction of Brompheniramine with Human Serum Albumin

AU - Tardioli, S.

AU - mr. Lammers, I.

AU - Hooijschuur, J.H.

AU - Ariese, F.

AU - van der Zwan, G.

AU - Gooijer, C.

PY - 2012

Y1 - 2012

N2 - Binding of the antihistamine drug brompheniramine (BPA) to human serum albumin (HSA) is studied by measuring quenching of the fluorescence and room temperature phosphorescence (RTP) of tryptophan. The modified Stern-Volmer equation was used to derive association constants and accessible fractions from the steady-state fluorescence data. Decay associated spectra (DAS) revealed three tryptophan fluorescence lifetimes, indicating the presence of three HSA conformations. BPA causes mainly static quenching of the long-living, solvent-exposed conformer. RTP spectra and lifetimes, recorded under deoxygenated conditions in the presence of 0.2 M KI, provided additional kinetic information about the HSA-BPA interactions. Fluorescence DAS that were also recorded in the presence of 0.2 M KI revealed that the solvent-exposed conformer is the major contributor to the RTP signal. The phosphorescence quenching is mostly dynamic at pH 7 and mostly static at pH 9, presumably related to the protonation state of the alkylamino chain of BPA. This provides direct insight into the binding mode of the antihistamine drug, as well as kinetic information at both the nanosecond and the millisecond time scales. © 2012 American Chemical Society.

AB - Binding of the antihistamine drug brompheniramine (BPA) to human serum albumin (HSA) is studied by measuring quenching of the fluorescence and room temperature phosphorescence (RTP) of tryptophan. The modified Stern-Volmer equation was used to derive association constants and accessible fractions from the steady-state fluorescence data. Decay associated spectra (DAS) revealed three tryptophan fluorescence lifetimes, indicating the presence of three HSA conformations. BPA causes mainly static quenching of the long-living, solvent-exposed conformer. RTP spectra and lifetimes, recorded under deoxygenated conditions in the presence of 0.2 M KI, provided additional kinetic information about the HSA-BPA interactions. Fluorescence DAS that were also recorded in the presence of 0.2 M KI revealed that the solvent-exposed conformer is the major contributor to the RTP signal. The phosphorescence quenching is mostly dynamic at pH 7 and mostly static at pH 9, presumably related to the protonation state of the alkylamino chain of BPA. This provides direct insight into the binding mode of the antihistamine drug, as well as kinetic information at both the nanosecond and the millisecond time scales. © 2012 American Chemical Society.

U2 - 10.1021/jp300055c

DO - 10.1021/jp300055c

M3 - Article

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SN - 1520-6106

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