Overcoming the low relaxivity of gadofosveset at high field with spin locking

O. C. Richardson, M. L J Scott, S. F. Tanner, J. C. Waterton, D. L. Buckley

    Research output: Contribution to journalArticlepeer-review


    The contrast agent gadofosveset, which binds reversibly to serum albumin, has a high longitudinal relaxivity at lower magnetic fields (≤3.0 T) but a much lower relaxivity at high fields. Spin locking is sensitive to macromolecular content; it is hypothesized that combining this technique with the albumin-binding properties of gadofosveset may enable increased relaxivity at high fields. In vitro measurements at 4.7 T found significantly higher spin-lock relaxation rates, R1ρ (1/T1ρ), when gadofosveset was serum albumin-bound than when unbound. R1ρ values for a nonbinding contrast agent (gadopentetate dimeglumine) in serum albumin were similar to those for unbound gadofosveset. R2 (1/T 2) values were also significantly higher at 4.7 T for serum albumin-bound gadofosveset than for unbound. Spin locking at high field generates significantly higher relaxation rates for gadofosveset than conventional contrast agents and may provide a method for differentiating free and bound molecules at these field strengths. Magn Reson Med, 2012. © 2011 Wiley Periodicals, Inc.
    Original languageEnglish
    Pages (from-to)1234-1238
    Number of pages4
    JournalMagnetic Resonance in Medicine
    Issue number4
    Publication statusPublished - Oct 2012


    • gadofosveset
    • relaxivity
    • spin locking
    • T1ρ


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