A calix[4]pyrrole (1) bearing a quaternary ammonium pendant via its meso phenoxy linker has been synthesized as the bromide salt form. It was revealed by ¹H NMR spectroscopic analyses performed in DMSO-d₆ that receptor 1 binds F^- with high affinity and selectivity over other halide anions. The binding of receptor 1•Br^- with F^- and Cltakes place by anion metathesis with the anions including F^- and Cl^-.

We study optical quantum transition line widths in relation to magnetic field dependence properties of the electrons confined in an infinite square well potential system between z = 0 and z = L_z in the z - direction. We consider two systems-one is subject to right circularly oscillating external fields and the other is subject to left circularly oscillatory external fields. Our results indicate that the line widths of right circularly oscillating external fields is larger than the line widths of left, while the opposite result is obtained for the line widths.

Apolipoprotein B-100 (apo B-100), the main protein component that makes up LDL (Low density lipoprotein), consists of 4,536 amino acids and serves to combine with the LDL receptor. The oxidized LDL peptides by malondialdehyde (MDA) or acetylation in vivo act as immunoglobulin (Ig) antigens and peptide groups were classified into 7 peptide groups with subsequent 20 amino acids (P1-P302). The biomimetic peptide P143 (IALDD AKINF NEKLS QLQTY) out of C-group peptides carrying the highest value of IgG antigens were selected for structural studies that may provide antigen specificity. Experimental results show that P143 has β-sheet in Ile[1]-Asn[9] and α-helice in Gln[16]-Tyr[20] structure. Homonuclear 2D-NMR (COSY, TOCSY, NOESY) experiments were carried out for NMR signal assignments and structure determination for P143. On the basis of these completely assigned NMR spectra and proton distance information, distance geometry (DG) and molecular dynamic (MD) were carried out to determine the structures of P143. The proposed structure was selected by comparisons between experimental NOE spectra and back-calculated 2D NOE results from determined structure showing acceptable agreement. The total Root-Mean-Square-Deviation (RMSD) value of P143 obtained upon superposition of all atoms were in the set range. The solution state P143 has a mixed structure of pseudo α-helix and β-turn(Phe[10] to Glu[12]). These results are well consistent with calculated structure from experimental data of NOE spectra. Structural studies based on NMR may contribute to the prevent oxidation studies of atherosclerosis and observed conformational characteristics of apo B-100 in LDL using monoclonal antibodies.

In the developed NMR hyperpolarization techniques, Signal amplification by reversible exchange (SABRE) technique is thought to be a promising method to overcome the low sensitivity of bio-NMR/MRI. Most experiments using SABRE have been done in methanol, which is biologically harmful solvent. Therefore, more biological friendly solvent, such as ethanol can be more appropriate solvent to be applicable in bio-NMR and MRI. As the proof of concept, successful hyperpolarization on pyridine via SABRE is carried out in ethanol and its enhancement factor is calculated to be more than 150 folds. To investigate more about its possibility of hyperpolarization in different alcohol solvents, methanol and propanol are used for SABRE in the same condition. The overall polarization trend in different external magnetic field is similar but its polarization number is decreased with higher molecular weight solvents (the order from methanol to propanol). This result indicates that the efficiency of SABRE is different from solvent system despite its same functional group and similar properties. Higher para-hydrogen concentration, higher partial pressure of para-hydrogen, and deuterated solvent can increase the hyperpolarization in any solvents. With these series of successful SABRE results, future studies on SABRE in more biofriendly environment, on more various solvent systems, and with more substrates are needed and it will be the firm basis for applying the SABRE system on the future bio-NMR/MRI.