Biomedical subjects

Jian Zhi Hu

Publications and source records attributed to Jian Zhi Hu.

7 recordsLinked to original sources

PubMed2006

(1)H relaxation times of metabolites in biological samples obtained with nondestructive ex-vivo slow-MAS NMR.

Methods suitable for measuring (1)H relaxation times such as T(1), T(2) and T(1rho) of metabolites in small, intact biological objects including live cells, excised organs and tissues, oil seeds etc. are developed in this work. This was achieved by combining inversion-recovery, spin-echo, or a spin-lock segment with the phase-adjusted spinning sideband (PASS) technique, which was applied at low sample-spinning rates. Here, PASS was used to produce high-resolution (1)H spectra in a nondestructive way so that the relaxation parameters of individual metabolite could be determined. The methodologies were demonstrated by measuring (1)H T(1), T(2), and T(1rho) of metabolites in excised rat liver at a spinning rate of 40 Hz.

Animals↗

PubMed2005

Line narrowing in 1H MAS spectrum of mesoporous silica by removing adsorbed H2O using N2.

The peaks for silanol protons in the high-resolution (1)H NMR spectrum obtained on mesoporous silica materials may be broadened and shifted downfield by hydrogen bonding with adsorbed water molecules. Overlapping of the resonance for hydrogen-bonded silanol with the corresponding broad peak due to hydrogen-bonded water may further complicate the spectrum. These complications hamper a quantitative analysis of the spectra for these and similar materials. It is demonstrated in this paper that adsorbed water can be removed by exposing the sample to dry N(2) during magic angle spinning. This results in significant line narrowing for the silanol protons in the (1)H MAS spectrum. The enhanced spectral resolution makes it possible to quantify the various hydroxyl groups in a complex metal-oxide catalyst. Results obtained on tungsten oxide supported on SBA-15 mesoporous silica materials are reported. Additionally, the proton chemical shift of tungsten hydroxyl is identified for the first time.

Adsorption↗

PubMed2004

Dynamic high-resolution 1H and 31P NMR spectroscopy and 1H T2 measurements in postmortem rabbit muscles using slow magic angle spinning.

Postmortem changes in rabbit muscle tissue with different glycogen status (normal vs low) were followed continuously from 13 min postmortem until 8 h postmortem and again 20 h postmortem using simultaneous magic angle spinning (1)H and (31)P NMR spectroscopy together with measurement of the transverse relaxation time, T(2), of the muscle water. The (1)H metabolite spectra were measured using the phase-altered spinning sidebands (PASS) technique at a spinning rate of 40 Hz. pH values calculated from the (31)P NMR spectra using the chemical shifts of the C-6 line of histidine in the (1)H spectra and the chemical shifts of inorganic phosphate in the (31)P spectra confirmed the different muscle glycogen status in the tissues. High-resolution (1)H spectra obtained from the PASS technique revealed the presence of a new resonance line at approximately 6.8 ppm during the postmortem period, which were absent in muscles with low muscle glycogen content. This new resonance line may originate from the aminoprotons in creatine, and its appearance may be a result of a pH effect on the exchange rate between the amino and the water protons and thereby the NMR visibility. Alternatively, the new resonance line may originate from the aromatic protons in tyrosine, and its appearance may be a result of a pH-induced protein unfolding exposing hydrophobic amino acid residues to the aqueous environment. Further studies are needed to evaluate these hypotheses. Finally, distributed analysis of the water T(2) relaxation data revealed three relaxation populations and an increase in the population believed to reflect extramyofibrillar water through the postmortem period. This increase was significantly reduced (p < 0.0001) in samples from animals with low muscle glycogen content, indicating that the pH is controlling the extent of postmortem expulsion of water from myofibrillar structures. The significance of the postmortem increase in the amount extramyofibrillar water on the water-holding capacity was verified by centrifugation, which showed a reduced centrifugation loss in muscles with low preslaughter glycogen status (0.9 vs 1.9%, p = 0.07).

Animals↗

PubMed2003

High-resolution 1H NMR spectroscopy in a live mouse subjected to 1.5 Hz magic angle spinning.

It is demonstrated that the resolution of the (1)H NMR metabolite spectrum in a live mouse can be significantly enhanced by an ultraslow magic angle spinning of the animal combined with a modified phase-corrected magic angle turning (PHORMAT) pulse sequence. Proton NMR spectra were measured of the torso and the top part of the belly of a female BALBc mouse in a 2 T field while spinning the animal at a speed of 1.5 Hz. It was found that even in this relatively low field, with PHORMAT an isotropic spectrum is obtained with line widths that are a factor of 4.6 smaller than those obtained in a stationary mouse. It is concluded that in vivo PHORMAT has the potential to significantly increase the utility of (1)H NMR spectroscopy for biochemical and biomedical animal research.

Animals↗

PubMed2003

Sensitivity-enhanced phase-corrected ultra-slow magic angle turning using multiple-echo data acquisition.

The increase in the sensitivity of the phase-corrected magic angle turning (PHORMAT) experiment at ultra-slow spinning rates by means of multiple-echo data acquisition (ME-PHORMAT) is evaluated. This is achieved by replacing the acquisition dimension in the original experiment with a train of equally spaced pi-pulses. It is shown that the echoes following the odd and even pi-pulses in the CPMG train must be processed differently in order to avoid spectral distortions. The method is illustrated for 13C CP-ME-PHORMAT on solid 1,2,3-trimethoxybenzene and for 1H ME-PHORMAT on excised rat liver tissue, both at a sample-spinning rate of 1.3 Hz. Sensitivity enhancements of a factor 4 for the solid and 2.3 for the liver were obtained. Finally, it is shown that with ME-PHORMAT one of the two RF pulse sequences, in standard PHORMAT used to obtain a pure absorption mode 2D spectrum, can be eliminated, thus reducing the usually long measuring time by a factor 2.

Algorithms↗

PubMed2002

High-resolution 1H NMR spectroscopy in rat liver using magic angle turning at a 1 Hz spinning rate.

It is demonstrated that a high-resolution (1)H NMR spectrum of excised rat liver can be obtained using the technique of magic angle turning (MAT) at a sample spinning rate of 1 Hz. A variant of the phase-corrected MAT (PHORMAT) pulse sequence that includes a water suppression segment was developed for the investigation. The spectral resolution achieved with PHORMAT approaches that obtained from a standard magic angle spinning (MAS) experiment at a spinning rate of several kHz. With such ultra-slow spinning, tissue and cell damage associated with the standard MAS experiment is minimized or eliminated. The technique is potentially useful for obtaining high-resolution (1)H spectra in live animals.

Animals↗

PubMed2002

The evaluation of different MAS techniques at low spinning rates in aqueous samples and in the presence of magnetic susceptibility gradients.

UNLABELLED: It was recently demonstrated that the nuclear magnetic resonance (NMR) linewidths for stationary biological samples are dictated mainly by magnetic susceptibility gradients, and that phase-altered spinning sideband (PASS) and phase-corrected magic angle turning (PHORMAT) solid-state NMR techniques employing slow and ultra-slow magic angle spinning (MAS) frequencies can be used to overcome the static susceptibility broadening to yield high-resolution, spinning sideband (SSB)-free 1H NMR spectra [Magn. Reson. Med. 46 (2001) 213; 47 (2002) 829]. An additional concern is that molecular diffusion in the presence of the susceptibility gradients may limit the minimum useful MAS frequency by broadening the lines and reducing SSB suppression at low spinning frequencies. In this article the performance of PASS, PHORMAT, total sideband suppression (TOSS), and standard MAS techniques were evaluated as a function of spinning frequency. To this end, 300MHz (7.05T) 1H NMR spectra were acquired via PASS, TOSS, PHORMAT, and standard MAS NMR techniques for a 230-microm-diameter spherical glass bead pack saturated with water. The resulting strong magnetic susceptibility gradients result in a static linewidth of about 3.7kHz that is larger than observed for a natural biological sample, constituting a worst-case scenario for examination of susceptibility broadening effects. RESULTS: (I) TOSS produces a distorted centerband and fails in suppressing the SSBs at a spinning rate below approximately 1kHz. (II) Standard MAS requires spinning speeds above a few hundred Hz to separate the centerband from the SSBs. (III) PASS produces nearly SSB-free spectra at spinning speeds as low as 30Hz, and is only limited by T(2)-induced signal losses. (IV) With PHORMAT, a SSB-free isotropic projection is obtained at any spinning rate, even at an ultra-slow spinning rate as slow as 1Hz. (V) It is found empirically that the width of the isotropic peak is proportional to F(-x), where F is the spinning frequency, and x=2 for MAS, 0.84 for PASS, and 0.5 for PHORMAT.

Magnetic Resonance Spectroscopy↗