Molecular factors that determine Curie spin relaxation in dysprosium complexes.
Dysprosium complexes can serve as transverse relaxation (T(2)) agents for water protons through chemical exchange and the Curie spin relaxation mechanism. Using a pair of matched dysprosium(III) complexes, Dy-L1 (contains one inner-sphere water) and Dy-L2 (no inner-sphere water), it is shown that the transverse relaxation of bulk water is predominantly an inner-sphere effect. The kinetics of water exchange at Dy-L1 were determined by (17)O NMR. Proton transverse relaxation by Dy-L1 at high fields is governed primarily through a large chemical shift difference between free and bound water. Dy-L1 forms a noncovalent adduct with human serum albumin which dramatically lengthens the rotational correlation time, tau(R), causing the dipole-dipole component of the Curie spin mechanism to become significant and transverse relaxivity to increase by 3-8 times that of the unbound chelate. These findings aid in the design of new molecular species as efficient r(2) agents.
Caravan
P
P
EPIX Medical, Inc., Cambridge, Massachusetts 02142-1118, USA. pcaravan@epixmed.com
Greenfield
M T
MT
Bulte
J W
JW
D003287:Contrast Media; D004419:Dysprosium / Q000737:chemistry*; D006801:Humans; D008279:Magnetic Resonance Imaging / Q000379:methods; D012709:Serum Albumin; D014867:Water
D003287:Contrast Media; D012709:Serum Albumin; D014867:Water; D004419:Dysprosium