Lipid magnetic resonance imaging contrast agent interactions: A spin- labeling and a multifrequency EPR study

Journal of the American Chemical Society

Volumn 120, Issue 20, 1998, Pages 5060-5072

  Smirnova, Tatyana I ^a   Smirnov, Alex I ^a   Belford, R L ^a   Clarkson, R B ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CONTRAST MEDIUM;

ARTICLE; CONTRAST ENHANCEMENT; DIAGNOSTIC VALUE; ELECTRON SPIN RESONANCE; LIPOPHILICITY; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE IMAGING;

EID: 0032572062     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja973427n     Document Type: Article

References (75)

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22. 3+ - spin-label interactions. Also, spin polarization effects, which are important for the relaxation of the radical pairs, are considered negligible for the fast-averaging paramagnetic metal ion - spin-label interactions. Other relevant literature concerns EPR of biradicals (for a review see, e.g.. Luckhurst, G. R. In Spin Labeling. Theory and Applications; Berliner, L. J., Ed.; Academic Press: NY, 1976; pp 133-183) and double-spin-labeled proteins. Some labels can be rigidly attached to proteins and electron-electron dipolar coupling can be clearly resolved from CW EPR spectra, especially at high magnetic fields (Hustedt, E. J.; Smirnov, A. I.; Laub, C. F.; Cobb, C. E.; Beth, A. H. Biophys. J. 1997, 74, 1861-1877). In contrast, rotational motion of flexibly attached labels with respect to the protein backbone causes in some averaging of dipole-dipole interactions. This averaging results in a homogeneous broadening across the EPR spectrum, which was modeled by convolution with a Lorentzian function and interpreted using Abraham's results (Mchaourab, H. S.; Oh, K. J.; Fang, C. J.; Hubbel, W. L. Biochemistry 1997, 36, 307-316).
23. 3+ - spin-label interactions. Also, spin polarization effects, which are important for the relaxation of the radical pairs, are considered negligible for the fast-averaging paramagnetic metal ion - spin-label interactions. Other relevant literature concerns EPR of biradicals (for a review see, e.g.. Luckhurst, G. R. In Spin Labeling. Theory and Applications; Berliner, L. J., Ed.; Academic Press: NY, 1976; pp 133-183) and double-spin-labeled proteins. Some labels can be rigidly attached to proteins and electron-electron dipolar coupling can be clearly resolved from CW EPR spectra, especially at high magnetic fields (Hustedt, E. J.; Smirnov, A. I.; Laub, C. F.; Cobb, C. E.; Beth, A. H. Biophys. J. 1997, 74, 1861-1877). In contrast, rotational motion of flexibly attached labels with respect to the protein backbone causes in some averaging of dipole-dipole interactions. This averaging results in a homogeneous broadening across the EPR spectrum, which was modeled by convolution with a Lorentzian function and interpreted using Abraham's results (Mchaourab, H. S.; Oh, K. J.; Fang, C. J.; Hubbel, W. L. Biochemistry 1997, 36, 307-316).
24. 3+ - spin-label interactions. Also, spin polarization effects, which are important for the relaxation of the radical pairs, are considered negligible for the fast-averaging paramagnetic metal ion - spin-label interactions. Other relevant literature concerns EPR of biradicals (for a review see, e.g.. Luckhurst, G. R. In Spin Labeling. Theory and Applications; Berliner, L. J., Ed.; Academic Press: NY, 1976; pp 133-183) and double-spin-labeled proteins. Some labels can be rigidly attached to proteins and electron-electron dipolar coupling can be clearly resolved from CW EPR spectra, especially at high magnetic fields (Hustedt, E. J.; Smirnov, A. I.; Laub, C. F.; Cobb, C. E.; Beth, A. H. Biophys. J. 1997, 74, 1861-1877). In contrast, rotational motion of flexibly attached labels with respect to the protein backbone causes in some averaging of dipole-dipole interactions. This averaging results in a homogeneous broadening across the EPR spectrum, which was modeled by convolution with a Lorentzian function and interpreted using Abraham's results (Mchaourab, H. S.; Oh, K. J.; Fang, C. J.; Hubbel, W. L. Biochemistry 1997, 36, 307-316).
25. 3+ - spin-label interactions. Also, spin polarization effects, which are important for the relaxation of the radical pairs, are considered negligible for the fast-averaging paramagnetic metal ion - spin-label interactions. Other relevant literature concerns EPR of biradicals (for a review see, e.g.. Luckhurst, G. R. In Spin Labeling. Theory and Applications; Berliner, L. J., Ed.; Academic Press: NY, 1976; pp 133-183) and double-spin-labeled proteins. Some labels can be rigidly attached to proteins and electron-electron dipolar coupling can be clearly resolved from CW EPR spectra, especially at high magnetic fields (Hustedt, E. J.; Smirnov, A. I.; Laub, C. F.; Cobb, C. E.; Beth, A. H. Biophys. J. 1997, 74, 1861-1877). In contrast, rotational motion of flexibly attached labels with respect to the protein backbone causes in some averaging of dipole-dipole interactions. This averaging results in a homogeneous broadening across the EPR spectrum, which was modeled by convolution with a Lorentzian function and interpreted using Abraham's results (Mchaourab, H. S.; Oh, K. J.; Fang, C. J.; Hubbel, W. L. Biochemistry 1997, 36, 307-316).
26. 3+ - spin-label interactions. Also, spin polarization effects, which are important for the relaxation of the radical pairs, are considered negligible for the fast-averaging paramagnetic metal ion - spin-label interactions. Other relevant literature concerns EPR of biradicals (for a review see, e.g.. Luckhurst, G. R. In Spin Labeling. Theory and Applications; Berliner, L. J., Ed.; Academic Press: NY, 1976; pp 133-183) and double-spin-labeled proteins. Some labels can be rigidly attached to proteins and electron-electron dipolar coupling can be clearly resolved from CW EPR spectra, especially at high magnetic fields (Hustedt, E. J.; Smirnov, A. I.; Laub, C. F.; Cobb, C. E.; Beth, A. H. Biophys. J. 1997, 74, 1861-1877). In contrast, rotational motion of flexibly attached labels with respect to the protein backbone causes in some averaging of dipole-dipole interactions. This averaging results in a homogeneous broadening across the EPR spectrum, which was modeled by convolution with a Lorentzian function and interpreted using Abraham's results (Mchaourab, H. S.; Oh, K. J.; Fang, C. J.; Hubbel, W. L. Biochemistry 1997, 36, 307-316).
27. 3+ - spin-label interactions. Also, spin polarization effects, which are important for the relaxation of the radical pairs, are considered negligible for the fast-averaging paramagnetic metal ion - spin-label interactions. Other relevant literature concerns EPR of biradicals (for a review see, e.g.. Luckhurst, G. R. In Spin Labeling. Theory and Applications; Berliner, L. J., Ed.; Academic Press: NY, 1976; pp 133-183) and double-spin-labeled proteins. Some labels can be rigidly attached to proteins and electron-electron dipolar coupling can be clearly resolved from CW EPR spectra, especially at high magnetic fields (Hustedt, E. J.; Smirnov, A. I.; Laub, C. F.; Cobb, C. E.; Beth, A. H. Biophys. J. 1997, 74, 1861-1877). In contrast, rotational motion of flexibly attached labels with respect to the protein backbone causes in some averaging of dipole-dipole interactions. This averaging results in a homogeneous broadening across the EPR spectrum, which was modeled by convolution with a Lorentzian function and interpreted using Abraham's results (Mchaourab, H. S.; Oh, K. J.; Fang, C. J.; Hubbel, W. L. Biochemistry 1997, 36, 307-316).
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