On the philosophy of optimizing contrast agents: an analysis of 1H NMRD profiles and ESR lineshapes of the Gd(III)complex MS-325 + HSA
2004 (English)In: Journal of magnetic resonance (San Diego, Calif. 1997: Print), ISSN 1090-7807, E-ISSN 1096-0856, Vol. 167, no 1, 147-160 p.Article in journal (Refereed) Published
A generalization of the modified SBM theory is developed in closed analytical form. The theory is applied to describe the paramagnetically enhanced water proton spin–lattice relaxation rates of the aqueous-systems containing a gadolinium(S=7/2) complex(MS-325) in the presence or absence of human serum albumin (HSA). MS-325 binds to HSA: in the absence of the protein the reorientational time, τR, is short, but when HSA is added τR becomes much longer. In this way, the effect of reorientational motion, static (Δs), and transient (Δt) zero-field splitting (ZFS) interactions on both the water proton relaxivity and the Gd ESR lineshapes are investigated.
Two dynamic models of electron spin relaxation are presented, characterized by transient and static ZFS-interactions. X-, Q-, and W-bands ESR spectra of MS-325+HSA are analyzed in order to describe the effect on the electron spin system upon binding to a macromolecule. A computer program based on this theory is developed which calculates solvent water proton T1 NMRD profiles and the corresponding X-, Q-, U-, and W-bands ESR lineshapes.
Place, publisher, year, edition, pages
San Diego: Academic Press , 2004. Vol. 167, no 1, 147-160 p.
IdentifiersURN: urn:nbn:se:umu:diva-14778DOI: 10.1016/j.jmr.2003.12.006OAI: oai:DiVA.org:umu-14778DiVA: diva2:154450