The relaxation of 1 H nuclei due to their interaction with quadrupolar 14 N nuclei in gel structures is measured using fast field-cycling NMR. This phenomenon called quadrupolar dips has been reported in different 1 H-14 N bond-rich species. In this study, we have studied quadrupolar dips in fibrin, an insoluble protein that is the core matrix of thrombi. Fibrin was formed by the addition of thrombin to fibrinogen in 0.2% agarose gel. T 1 -dispersion curves were measured using fast fieldcycling NMR relaxometry, over the field range of 1.5-3.5 MHz (proton Larmor frequency), and were analyzed using a curvefitting algorithm. A linear increase of signal amplitude with increasing fibrin concentration was observed. This agrees with the current theory that predicts a linear relationship of signal amplitude with the concentration of contributing 14 N spins in the sample. Interestingly, fibrin formation gave rise to the signal, regardless of crosslinking induced by the transglutaminase factor XIIIa. To investigate the effect of proteins that might be trapped in the thrombi in vivo, the plasma protein albumin was added to the fibrin gel, and an increase in the quadrupolar signal amplitude was observed. This study can potentially be useful for thrombi classification by fast field-cycling MRI techniques. Magn Reson Med 67:1453-1457, 2012. V C 2011 Wiley Periodicals, Inc.
Key words: fast field cycling; relaxometry; fibrin; quadrupolar dipThe technique of fast field cycling that involves rapidly changing the magnetic field during a pulse sequence has developed steadily during the last three decades (1). The ability to investigate the behavior of a sample over a range of magnetic strengths has proved useful to investigate molecular dynamics (2), in particular for the identification of quadrupole dips in a way that cannot be examined using fixed-field NMR (3). With the recent incorporation of fast field-cycling techniques into MRI, this technique opens up even more possibilities on living tissues and organic materials (4).In this study, we focus on the 1 H-14 N quadrupole dips previously observed in several experiments (5). Quadrupole dips and related phenomena have been previously measured using a number of methods and various types of sample, such as amino acids and nucleic bases (6), liquid crystalline material in the solid state (7), or monitoring of the concentration of immobilized protein (8).As the spin of the 14 N nucleus is 1, it possesses a quadrupolar moment that makes it relax very efficiently by coupling with the lattice. Magnetization transfer from water protons to 14 N can happen at a short range and leads to an increase in water proton relaxation (9). This additional relaxation pathway occurs when one of the nuclear quadrupolar energy levels matches the 1 H Larmor frequency, generating dips in the T 1 -dispersion curve called quadrupole dips at three distinct magnetic fields (or Larmor frequencies), typically 16, 49, and 65 mT (9). However, this process can only happen when the NH bond is sufficiently immobilize...