A 19F NMR study of lomefloxacin in human erythrocytes and its interaction with hemoglobin

Sheila R. Knaub; Melanie J. Priston; Martha D. Morton; Joseph D. Slechta; David G. Vander Velde; Christopher M. Riley

doi:10.1016/0731-7085(95)01509-J

A ¹⁹F NMR study of lomefloxacin in human erythrocytes and its interaction with hemoglobin

Sheila R. Knaub, Melanie J. Priston, Martha D. Morton, Joseph D. Slechta, David G. Vander Velde, Christopher M. Riley^*

^*Corresponding author for this work

Peninsula Medical School

University of Kansas

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

Abstract

¹⁹F NMR spectroscopy of a model fluoroquinolone, lomefloxacin, in an erythrocyte suspension showed separate resonances for the intra- and extra-cellular compartments. The intra-cellular peak revealed significant line broadening of the fluorine signals of lomefloxacin. Line broadening also occurred in the presence of oxyhemoglobin (HbO₂), hematin, globin and iron. This evidence indicated that lomefloxacin interacted with these compounds; however, ultrafiltration experiments indicated that there was only weak binding (5%) of lomefloxacin to HbO₂. ¹⁹F and ³¹P NMR spectroscopy revealed that lomefloxacin may compete with 2,3-diphosphoglycerate for its binding site on HbO₂. An apparent partition coefficient of 1.90 ± 0.15 was observed for lomefloxacin in human erythrocytes, utilizing LC analysis.

Original language	English
Pages (from-to)	1225-1233
Number of pages	9
Journal	Journal of Pharmaceutical and Biomedical Analysis
Volume	13
Issue number	10
DOIs	https://doi.org/10.1016/0731-7085(95)01509-J
Publication status	Published - Sept 1995

ASJC Scopus subject areas

Analytical Chemistry
Pharmaceutical Science
Drug Discovery
Spectroscopy
Clinical Biochemistry

Keywords

2,3-Diphosphoglycerate
F NMR
P NMR
Erythrocyte
Fluoroquinolone
Hemoglobin binding
Lomefloxacin

Access to Document

10.1016/0731-7085(95)01509-J

Cite this

@article{8c611a9688804b789359fda4fde074af,

title = "A 19F NMR study of lomefloxacin in human erythrocytes and its interaction with hemoglobin",

abstract = "19F NMR spectroscopy of a model fluoroquinolone, lomefloxacin, in an erythrocyte suspension showed separate resonances for the intra- and extra-cellular compartments. The intra-cellular peak revealed significant line broadening of the fluorine signals of lomefloxacin. Line broadening also occurred in the presence of oxyhemoglobin (HbO2), hematin, globin and iron. This evidence indicated that lomefloxacin interacted with these compounds; however, ultrafiltration experiments indicated that there was only weak binding (5%) of lomefloxacin to HbO2. 19F and 31P NMR spectroscopy revealed that lomefloxacin may compete with 2,3-diphosphoglycerate for its binding site on HbO2. An apparent partition coefficient of 1.90 ± 0.15 was observed for lomefloxacin in human erythrocytes, utilizing LC analysis.",

keywords = "2,3-Diphosphoglycerate, F NMR, P NMR, Erythrocyte, Fluoroquinolone, Hemoglobin binding, Lomefloxacin",

author = "Knaub, {Sheila R.} and Priston, {Melanie J.} and Morton, {Martha D.} and Slechta, {Joseph D.} and {Vander Velde}, {David G.} and Riley, {Christopher M.}",

year = "1995",

month = sep,

doi = "10.1016/0731-7085(95)01509-J",

language = "English",

volume = "13",

pages = "1225--1233",

journal = "Journal of Pharmaceutical and Biomedical Analysis",

issn = "0731-7085",

publisher = "Elsevier B.V.",

number = "10",

}

TY - JOUR

T1 - A 19F NMR study of lomefloxacin in human erythrocytes and its interaction with hemoglobin

AU - Knaub, Sheila R.

AU - Priston, Melanie J.

AU - Morton, Martha D.

AU - Slechta, Joseph D.

AU - Vander Velde, David G.

AU - Riley, Christopher M.

PY - 1995/9

Y1 - 1995/9

N2 - 19F NMR spectroscopy of a model fluoroquinolone, lomefloxacin, in an erythrocyte suspension showed separate resonances for the intra- and extra-cellular compartments. The intra-cellular peak revealed significant line broadening of the fluorine signals of lomefloxacin. Line broadening also occurred in the presence of oxyhemoglobin (HbO2), hematin, globin and iron. This evidence indicated that lomefloxacin interacted with these compounds; however, ultrafiltration experiments indicated that there was only weak binding (5%) of lomefloxacin to HbO2. 19F and 31P NMR spectroscopy revealed that lomefloxacin may compete with 2,3-diphosphoglycerate for its binding site on HbO2. An apparent partition coefficient of 1.90 ± 0.15 was observed for lomefloxacin in human erythrocytes, utilizing LC analysis.

AB - 19F NMR spectroscopy of a model fluoroquinolone, lomefloxacin, in an erythrocyte suspension showed separate resonances for the intra- and extra-cellular compartments. The intra-cellular peak revealed significant line broadening of the fluorine signals of lomefloxacin. Line broadening also occurred in the presence of oxyhemoglobin (HbO2), hematin, globin and iron. This evidence indicated that lomefloxacin interacted with these compounds; however, ultrafiltration experiments indicated that there was only weak binding (5%) of lomefloxacin to HbO2. 19F and 31P NMR spectroscopy revealed that lomefloxacin may compete with 2,3-diphosphoglycerate for its binding site on HbO2. An apparent partition coefficient of 1.90 ± 0.15 was observed for lomefloxacin in human erythrocytes, utilizing LC analysis.

KW - 2,3-Diphosphoglycerate

KW - F NMR

KW - P NMR

KW - Erythrocyte

KW - Fluoroquinolone

KW - Hemoglobin binding

KW - Lomefloxacin

UR - http://www.scopus.com/inward/record.url?scp=0028972678&partnerID=8YFLogxK

U2 - 10.1016/0731-7085(95)01509-J

DO - 10.1016/0731-7085(95)01509-J

M3 - Article

C2 - 8562594

AN - SCOPUS:0028972678

SN - 0731-7085

VL - 13

SP - 1225

EP - 1233

JO - Journal of Pharmaceutical and Biomedical Analysis

JF - Journal of Pharmaceutical and Biomedical Analysis

IS - 10

ER -