Relaxivity and binding of Mn2+ ions in solutions of phosphatidylserine vesicles.
We report the magnetic field dependence (NMRD profiles) of 1/T1 of solvent protons in solutions of unilamellar phosphatidylserine vesicles with added Mn2+ ions, including studies of the variation of the profiles with temperature, extent of coverage of available binding sites by Mn2+ ions, ionic strength, and competition with (nonparamagnetic) Ca2+ ions. ions. In addition, we sketch the theory of screening of the negative surface charges of the vesicles due to both specific binding of Mn2+ ions and nonspecific effects of other mobile solute ions. The major result is that the NMRD profiles, although qualitatively similar, vary systematically as the parameters of the solutions are altered, in a manner consistent with the theory of screening. The profiles of the Mn2+-vesicle complexes are much like those of Mn2+-protein complexes that have the ions in an octahedral ligand environment. In addition, we find that the profiles are similar to those reported for Mn2+ ions in packed liver cells and liver tissue, supporting a previous conjecture that available Mn2+ in liver binds to the polar head groups of cell membranes, saturating these sites before binding elsewhere. Again, it is evident that results for in vitro model systems can be extrapolated reliably to tissue behavior.
Koenig
S H
SH
IBM T. J. Watson Research Center, Yorktown Heights, New York 10598.
Brown
R D
RD
Kurland
R
R
Ohki
S
S
D003287:Contrast Media; D007477:Ions; D008081:Liposomes; D008279:Magnetic Resonance Imaging; D008345:Manganese; D010718:Phosphatidylserines
D003287:Contrast Media; D007477:Ions; D008081:Liposomes; D010718:Phosphatidylserines; D008345:Manganese