Magnetization transfer

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Magnetization transfer (MT), in NMR and MRI, refers to the transfer of nuclear spin polarization and/or spin coherence from one population of nuclei to another population of nuclei, and to techniques that make use of these phenomena. [1] There is some ambiguity regarding the precise definition of magnetization transfer, however the general definition given above encompasses all more specific notions. NMR active nuclei, those with non-zero spin, can be energetically coupled to one another under certain conditions. The mechanisms of nuclear-spin energy-coupling have been extensively characterized and are described in the following articles: Angular momentum coupling, Magnetic dipole–dipole interaction, J-coupling, Residual dipolar coupling, Nuclear Overhauser effect, Spin–spin relaxation, and Spin saturation transfer. Alternatively, some nuclei in a chemical system are labile and exchange between non-equivalent environments. A more specific example of this case is presented in the section Chemical Exchange Magnetization transfer.

Contents

In either case, magnetization transfer techniques probe the dynamic relationship between two or more distinguishable nuclei populations, in so far as energy exchange between the populations can be induced and measured in an idealized NMR experiment.

Chemical Exchange Magnetization transfer

In magnetic resonance imaging or NMR of macromolecular samples, such as protein solutions, at least two types of water molecules, free (bulk) and bound (hydration), are present. Bulk water molecules have many mechanical degrees of freedom, and motion of such molecules thus exhibits statistically averaged behavior. Because of this uniformity, most free water protons have resonance frequencies very near the average Larmor frequency of all such protons. On a properly acquired NMR spectrum this is seen as a narrow Lorentzian line (at 4.8 ppm, 20 C). Bulk water molecules are also relatively far from magnetic field perturbing macromolecules, such that free water protons experience a more homogeneous magnetic field, which results in slower transverse magnetization dephasing and a longer T2*. Conversely, hydration water molecules are mechanically constrained by extensive interactions with the local macromolecules and hence magnetic field inhomogeneities are not averaged out, which leads to broader resonance lines. This results in faster dephasing of the magnetization that produces the NMR signal and much shorter T2 values(<200 μs). Because the T2 values are so short, the NMR signal from the protons of bound water is not typically observed in MRI.

However, using an off-resonance saturation pulse to irradiate protons in the bound (hydration) population can have a detectable effect on the NMR signal of the mobile (free) proton pool. When a population of spins is saturated, such that the magnitude of the macroscopic magnetization vector approaches zero, there is no remaining spin polarization with which to produce an NMR signal. Longitudinal relaxation refers to the return of longitudinal spin polarization, which occurs at a rate described by T1. While the number of hydration water molecules may be insufficient to produce an observable signal, exchange of water molecules between the hydration and bulk population allows characterization of the hydration population, and measurement of the rate at which molecules are exchanging between bulk and bound sites. Such experiments are often termed saturation transfer or chemical exchange saturation transfer (CEST), because the signal of the bulk water is observed to decrease when the hydration population is saturated. Considering these techniques from the opposite perspective, that magnetization (i.e. spin polarization) is being transferred from the bulk water to the spin-saturated hydration population, allows one to conceptually unify chemical exchange methods with other techniques that transfer magnetization between nuclei populations. Since the extent of signal decay depends on the exchange rate between free and hydration water, MT can be used to provide an alternative contrast method in addition to T1,T2, and proton density differences.

MT is believed to be a nonspecific indicator of the structural integrity of the tissue being imaged.

An extension of MT, the magnetization transfer ratio (MTR) has been used in neuroradiology to highlight abnormalities in brain structures. (The MTR is (Mo-Mt)/Mo.)

A systematic modulation of the precise frequency offset for the saturation pulse can be plotted against the free-water signal to form a "Z-spectrum". This technique is often referred to as "Z-spectroscopy".

See also

Related Research Articles

The nuclear Overhauser effect (NOE) is the transfer of nuclear spin polarization from one population of spin-active nuclei to another via cross-relaxation. A phenomenological definition of the NOE in nuclear magnetic resonance spectroscopy (NMR) is the change in the integrated intensity of one NMR resonance that occurs when another is saturated by irradiation with an RF field. The change in resonance intensity of a nucleus is a consequence of the nucleus being close in space to those directly affected by the RF perturbation.

Hyperpolarization is the nuclear spin polarization of a material in a magnetic field far beyond thermal equilibrium conditions determined by the Boltzmann distribution. It can be applied to gases such as 129Xe and 3He, and small molecules where the polarization levels can be enhanced by a factor of 104-105 above thermal equilibrium levels. Hyperpolarized noble gases are typically used in magnetic resonance imaging (MRI) of the lungs. Hyperpolarized small molecules are typically used for in vivo metabolic imaging. For example, a hyperpolarized metabolite can be injected into animals or patients and the metabolic conversion can be tracked in real-time. Other applications include determining the function of the neutron spin-structures by scattering polarized electrons from a very polarized target (3He), surface interaction studies, and neutron polarizing experiments.

<span class="mw-page-title-main">Nuclear magnetic resonance spectroscopy</span> Laboratory technique

Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique to observe local magnetic fields around atomic nuclei. The sample is placed in a magnetic field and the NMR signal is produced by excitation of the nuclei sample with radio waves into nuclear magnetic resonance, which is detected with sensitive radio receivers. The intramolecular magnetic field around an atom in a molecule changes the resonance frequency, thus giving access to details of the electronic structure of a molecule and its individual functional groups. As the fields are unique or highly characteristic to individual compounds, in modern organic chemistry practice, NMR spectroscopy is the definitive method to identify monomolecular organic compounds.

Carbon-13 (C13) nuclear magnetic resonance is the application of nuclear magnetic resonance (NMR) spectroscopy to carbon. It is analogous to proton NMR and allows the identification of carbon atoms in an organic molecule just as proton NMR identifies hydrogen atoms. 13C NMR detects only the 13
C
 isotope. The main carbon isotope, 12
C
 is not detected. Although much less sensitive than 1H NMR spectroscopy, 13C NMR spectroscopy is widely used for characterizing organic and organometallic compounds.

Nuclear magnetic resonance spectroscopy of proteins is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes. The field was pioneered by Richard R. Ernst and Kurt Wüthrich at the ETH, and by Ad Bax, Marius Clore, Angela Gronenborn at the NIH, and Gerhard Wagner at Harvard University, among others. Structure determination by NMR spectroscopy usually consists of several phases, each using a separate set of highly specialized techniques. The sample is prepared, measurements are made, interpretive approaches are applied, and a structure is calculated and validated.

Two-dimensional nuclear magnetic resonance spectroscopy is a set of nuclear magnetic resonance spectroscopy (NMR) methods which give data plotted in a space defined by two frequency axes rather than one. Types of 2D NMR include correlation spectroscopy (COSY), J-spectroscopy, exchange spectroscopy (EXSY), and nuclear Overhauser effect spectroscopy (NOESY). Two-dimensional NMR spectra provide more information about a molecule than one-dimensional NMR spectra and are especially useful in determining the structure of a molecule, particularly for molecules that are too complicated to work with using one-dimensional NMR.

In MRI and NMR spectroscopy, an observable nuclear spin polarization (magnetization) is created by a homogeneous magnetic field. This field makes the magnetic dipole moments of the sample precess at the resonance (Larmor) frequency of the nuclei. At thermal equilibrium, nuclear spins precess randomly about the direction of the applied field. They become abruptly phase coherent when they are hit by radiofrequent (RF) pulses at the resonant frequency, created orthogonal to the field. The RF pulses cause the population of spin-states to be perturbed from their thermal equilibrium value. The generated transverse magnetization can then induce a signal in an RF coil that can be detected and amplified by an RF receiver. The return of the longitudinal component of the magnetization to its equilibrium value is termed spin-latticerelaxation while the loss of phase-coherence of the spins is termed spin-spin relaxation, which is manifest as an observed free induction decay (FID).

Insensitive nuclei enhancement by polarization transfer (INEPT) is a signal enhancement method used in NMR spectroscopy. It involves the transfer of nuclear spin polarization from spins with large Boltzmann population differences to nuclear spins of interest with lower Boltzmann population differences. INEPT uses J-coupling for the polarization transfer in contrast to Nuclear Overhauser effect (NOE), which arises from dipolar cross-relaxation. This method of signal enhancement was introduced by Ray Freeman in 1979. Due to its usefulness in signal enhancement, pulse sequences used in heteronuclear NMR experiments often contain blocks of INEPT or INEPT-like sequences.

<span class="mw-page-title-main">Spin echo</span> Response of spin to electromagnetic radiation

In magnetic resonance, a spin echo or Hahn echo is the refocusing of spin magnetisation by a pulse of resonant electromagnetic radiation. Modern nuclear magnetic resonance (NMR) and magnetic resonance imaging (MRI) make use of this effect.

During nuclear magnetic resonance observations, spin–lattice relaxation is the mechanism by which the longitudinal component of the total nuclear magnetic moment vector (parallel to the constant magnetic field) exponentially relaxes from a higher energy, non-equilibrium state to thermodynamic equilibrium with its surroundings (the "lattice"). It is characterized by the spin–lattice relaxation time, a time constant known as T1.

Nuclear magnetic resonance (NMR) in the geomagnetic field is conventionally referred to as Earth's field NMR (EFNMR). EFNMR is a special case of low field NMR.

In vivo magnetic resonance spectroscopy (MRS) is a specialized technique associated with magnetic resonance imaging (MRI).

Nuclear magnetic resonance decoupling is a special method used in nuclear magnetic resonance (NMR) spectroscopy where a sample to be analyzed is irradiated at a certain frequency or frequency range to eliminate fully or partially the effect of coupling between certain nuclei. NMR coupling refers to the effect of nuclei on each other in atoms within a couple of bonds distance of each other in molecules. This effect causes NMR signals in a spectrum to be split into multiple peaks. Decoupling fully or partially eliminates splitting of the signal between the nuclei irradiated and other nuclei such as the nuclei being analyzed in a certain spectrum. NMR spectroscopy and sometimes decoupling can help determine structures of chemical compounds.

<span class="mw-page-title-main">Nuclear magnetic resonance</span> Spectroscopic technique based on change of nuclear spin state

Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a strong constant magnetic field are perturbed by a weak oscillating magnetic field and respond by producing an electromagnetic signal with a frequency characteristic of the magnetic field at the nucleus. This process occurs near resonance, when the oscillation frequency matches the intrinsic frequency of the nuclei, which depends on the strength of the static magnetic field, the chemical environment, and the magnetic properties of the isotope involved; in practical applications with static magnetic fields up to ca. 20 tesla, the frequency is similar to VHF and UHF television broadcasts (60–1000 MHz). NMR results from specific magnetic properties of certain atomic nuclei. Nuclear magnetic resonance spectroscopy is widely used to determine the structure of organic molecules in solution and study molecular physics and crystals as well as non-crystalline materials. NMR is also routinely used in advanced medical imaging techniques, such as in magnetic resonance imaging (MRI).

Nucleic acid NMR is the use of nuclear magnetic resonance spectroscopy to obtain information about the structure and dynamics of nucleic acid molecules, such as DNA or RNA. It is useful for molecules of up to 100 nucleotides, and as of 2003, nearly half of all known RNA structures had been determined by NMR spectroscopy.

Nuclear magnetic resonance (NMR) logging is a type of well logging that uses the NMR response of a formation to directly determine its porosity and permeability, providing a continuous record along the length of the borehole.

Paramagnetic nuclear magnetic resonance spectroscopy Spectroscopy of paramagnetic compounds via NMR

Paramagnetic nuclear magnetic resonance spectroscopy refers to nuclear magnetic resonance (NMR) spectroscopy of paramagnetic compounds. Although most NMR measurements are conducted on diamagnetic compounds, paramagnetic samples are also amenable to analysis and give rise to special effects indicated by a wide chemical shift range and broadened signals. Paramagnetism diminishes the resolution of an NMR spectrum to the extent that coupling is rarely resolved. Nonetheless spectra of paramagnetic compounds provide insight into the bonding and structure of the sample. For example, the broadening of signals is compensated in part by the wide chemical shift range (often 200 ppm in 1H NMR). Since paramagnetism leads to shorter relaxation times (T1), the rate of spectral acquisition can be high.

MRI sequence

An MRI sequence in magnetic resonance imaging (MRI) is a particular setting of pulse sequences and pulsed field gradients, resulting in a particular image appearance.

<span class="mw-page-title-main">Cross-polarization</span> Spectroscopy technique

Cross-polarization, also known as proton-enhanced nuclear induction spectroscopy is a solid-state nuclear magnetic resonance (ssNMR) technique to transfer nuclear magnetization from different types of nuclei via heteronuclear dipolar interactions. The 1H-X cross-polarization dramatically improves the sensitivity of ssNMR experiments of most experiments involving spin-1/2 nuclei, capitalizing on the higher 1H polarisation, and shorter T1(1H) relaxation times. It was developed by Michael Gibby, Alexander Pines and Professor John S. Waugh at the Massachusetts Institute of Technology.

Hyperpolarized 129Xe gas magnetic resonance magnetic resonance imaging (MRI) is a medical imaging technique used to visualize the anatomy and physiology of body regions that are difficult to image with standard proton MRI. In particular, the lung, which lacks substantial density of protons, is particularly useful to be visualized with 129Xe gas MRI. This technique has promise as an early-detection technology for chronic lung diseases and imaging technique for processes and structures reliant on dissolved gases. 129Xe is a stable, naturally occurring isotope of xenon with 26.44% isotope abundance. It is one of two Xe isotopes, along with 131Xe, that has non-zero spin, which allows for magnetic resonance. 129Xe is used for MRI because its large electron cloud permits hyperpolarization and a wide range of chemical shifts. The hyperpolarization creates a large signal intensity, and the wide range of chemical shifts allows for identifying when the 129Xe associates with molecules like hemoglobin. 129Xe is preferred over 131Xe for MRI because 129Xe has spin 1/2, a longer T1, and 3.4 times larger gyromagnetic ratio.

References

  1. ↑ Rodríguez-Rodríguez, Aurora; Zaiss, Moritz; Esteban-Gómez, David; Angelovski, Goran; Platas-Iglesias, Carlos (2021). "Chapter 4. Metal Ion Complexes in Paramagnetic Chemical Exchange Saturation Transfer (ParaCEST)". Metal Ions in Bio-Imaging Techniques. Springer. pp. 101–135. doi:10.1515/9783110685701-010. S2CID   233710016.
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