• Bulletin of the Korean Chemical Society
• /
• v.32 no.7
• /
• pp.2193-2198
• /
• 2011

We prepared polycatenar 1H-imidazole amphiphiles having a structure in which a 1H-imidazole head was connected through a benzene ring to a pheny group having two or three oligo(ethylene glycol) chains and studied their supramolecular assembly by fluorescence spectroscopy, transmission electron microscopy (TEM) and atomic force microscopy (AFM). When the aqueous solutions of the amphiphiles ($5{\times}10^{-5}M{\sim}10^{-3}M$) were deposited onto a carbon-coated copper grid and dried, twisted structures with diameters of ~200-300 nm were imaged by TEM and AFM. We presume that the structures comprised a chain of the amphiphile dimers formed via successive hydrogen bonding between the 1H of the imidazole group and 3N of the neighboring one. In a solution of pH 4, entangled fibers with diameters of several nanometers were observed by TEM. In a pH 10 solution, film-like aggregates formed exclusively. The 1H-imidazole amphiphiles hydrolyzed tetraethoxysilane to induce gelation to form fibrous and spherical silica structures at neutral pH in aqueous solutions. No silica was formed when imidazole was used instead of the amphiphiles, suggesting that the selfassembled aggregates of the amphiphiles were responsible for the gelation.

• Bulletin of the Korean Chemical Society
• /
• v.18 no.1
• /
• pp.14-18
• /
• 1997

Sulconazole nitrate, C18H16Cl3N3O3S, crystallizes in monoclinic, space group C2/c, with a=14.401(1), b=8.051(1), c=34.861(2) Å, β=95.9(1)°, g=0.58 mm-1, Dc=1.523 g/cm3, Dm=1.522 g/cm3, F(000)=1888.0, and z=8. Intensities for 2460 unique reflections were measured on a CAD4 diffractometer with graphited-monochromated Mo-Kα radiation. The structure was solved by direct method and refined by full matrix least squares to a final R=0.071 for 2182 reflections (Io > 2σIo). The bond lengths and angles are comparable with the values found in the analogues imidazole derivatives. The 2,4-dichlorophenyl ring(A) and the p-chlorophenyl ring(B) are almost planar with different heights [dihedral angle 17.3°] while the imidazole ring(C) is nearly perpendicular to the two phenyl rings[dihedral angles about the two rings A, B are 110.8° and 96.1° respectively]. In order to understand the overall conformation we calculated the selected distances (l1, l2, l3) among the center of the three rings and considered the imaginary plan D[C(7), C(9) and C(16)]. The two polar group S(8) and N(19) do not have gauche conformation and l2 value (4.47 Å) is shorter than the other imidazole derivatives. One -NO3 group are hydrogen bonded the two neighbored sulconazole molecules. The molecular crystal packing is also formed by two hydrogen bondings and van der Waals forces.

• Journal of the Korean Chemical Society
• /
• v.38 no.1
• /
• pp.21-25
• /
• 1994

The proton affinities of substituted imidazoles, relevant to the binding of lexitropsins that contain imidazole ring to the base pair (G-C sequence) of minor groove of DNA, are studied with the aid of EHT calculations. It is shown that proton affinity of imidazole substituted at position $\alpha$ to the basic nitrogen is slightly larger than that of imidazole substituted at N for the methylimidazole. Proton affinities of N-substituted imidazoles are found to be larger than those of imidazoles substituted at position ${\alpha}$ for a selected set of the other derivatives. As predicted the proton affinity increases when electron-donating group is attached at position N of imidazole.

• Bulletin of the Korean Chemical Society
• /
• v.31 no.11
• /
• pp.3217-3220
• /
• 2010

The electronic structures and bonding configuration of histidine on Ge(100) have been investigated with various sample treatments using core-level photoemission spectroscopy (CLPES). Interpretation of the Ge 3d, C 1s, N 1s, and O 1s core level spectra being included in these systems revealed that both the imino nitrogen in the imidazole ring and the carboxyl group in the glycine moiety concurrently participate in the adsorption of histidine on a Ge(100) surface at 380 K. Moreover, we could clearly confirm that the imino nitrogen with a free lone pair in the imidazole group adsorbs on Ge(100) more strongly than the carboxyl group in the glycine moiety by examining systems annealed at various temperatures.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
• /
• 2000.05b
• /
• pp.265-268
• /
• 2000

We fabricated an IMI-O polymer containing an imidazole group that could form a complex structure between the monolayer and the metal ions at the air-water interface. Also. the monolayer behavior at the air-water interface and the surface morphology of metal-complexed Langmuir-Blodgett(LB) films were investigated by using Brewster angle microscopy(BAM) and Scanning Maxwell-stress Microscopy(SMM). The difference in the BAM and SMM images between the pure water and the aqueous metal ions is attributed to the interactions of the copolymers with the metal ions at the interface and the consequent change of the monolayer organization.

• Bulletin of the Korean Chemical Society
• /
• v.30 no.11
• /
• pp.2621-2625
• /
• 2009

To identify a non-acylguanidine NHE-1 inhibitor, an acylguanidne group was replaced with an imidazole group in the potent NHE-1 inhibitors with furan or benzothiphene core template, found from our previous studies. We synthesized and biologically evaluated 4-heteroaryl-2-amino-5-methylimidazole derivatives. All those imidazole compounds (16-18) represented the potent NHE-1 inhibitory activities, similar to the corresponding acylguanidine compounds.

• Proceedings of the Materials Research Society of Korea Conference
• /
• 1998.08a
• /
• pp.150.1-150
• /
• 1998

• Journal of the Korean Chemical Society
• /
• v.5 no.1
• /
• pp.33-37
• /
• 1961

We have shown that carboxy-peptidase destroys the biological activity of angiotensin octa-and deca-peptides. Since Proline occurs as the seventh amino acid from the amino end of the chain and since carboxypeptidase does not cleave proline from a peptid chain, it is evident that the heptapeptid H.asp-arg-val-tyr-ileu-his-pro.OH is formed by this hydrolysis. This peptide must then be biologically inactive. In order to determine whether the phenyl group of the C-terminal amino acid was the necessary requirement for biological activity of the octapeptide, $ala^8$ angiotensin octapeptide(amino acids of peptides numbered from amino end) was synthesized. For this synthesis the four dipeptides were prepared: carbobenzoxy-L-prolyl-L-alanine-P-nitrobenzyl-ester, m.p. $134-135^{\circ}C,$ carbobenzoxy-L-isoleucyl-imidazole benzyl-L-histidine methyl ester, m.p. $114-116^{\circ}C,$ carbobenzoxy-L-valyl-L-tyrosine hydrazide and carbobenzoxy B-benzyl-L-aspartyl-nitro-L-arginine. The first three dipeptides were obtained as crystalline compounds. Imidazole-benzyl-L-histidine was used in the hope that it would block the histidine imidazole against side reactions in steps subsequent to the formation of the C-terminal tetrapeptide. Also, it was through that the imidazole benzylated peptides would be easier to crystallize. This, however, was not the case. The tetrapeptide, carbobenzoxy-L-isoleucyl-L-im, benzyl-histidyl, L-prolyl-L-alanine-nitrobenzyl ester was not obtained in a crystalline form. Neither could the mono-or dihydrobromide of the tetrapeptide free base be induced to crystallize. Carbobenzoxy-L-valyl-L-tyrosine azide was condensed with the tetrapeptide free base to yield the protected hexapeptide; carbobenzoxy-L-valyl-L-tyrosyl-L-isoleucyl-L-im, benzyl, histidyl-L-Prolyl-L-alanine-nitrobenzyl ester. Upon removal of the carbobenzoxy group with hydrogen bromide in acetic acid an amorphous free base hexapeptide ester was obtained. This compound gave the correct C, H, N analysis and contained the six amino acids in the correct ratio. The octapeptide was obtained by condensing this hexapeptide with carbobenzoxy-B-benzyl-L-aspartyl-nitro, L-arginine using the mixed anhydride method of condensation. This amorphous product was proven to be homogenous by chromatography in two solvent systems and upon hydrolysis yielded the eight amino acids in correct ratio. The five protecting groups were removed from the octapeptide by hydrogenolysis over palladium black catalyst. Biological assay of the free peptide indicated that it possessed less than 0.1 per cent of both pressor and oxytocic activity of the phenylalanine8 angiotensin. This suggests that the phenyl group is a point of attachment between angiotensin and its biological receptor site.

• Bulletin of the Korean Chemical Society
• /
• v.22 no.11
• /
• pp.1197-1201
• /
• 2001

In the spectrum of uniformly 15N labeled cytochrome c3, the relative linewidths of the doublet peaks of the 15N-coupled imido proton of the coordinated imidazole group were reversed on oxidation. This inversion was explained by the interference relaxation process between the electron-proton dipolar and 15N-1H dipolear interactions. The inversion can be used to assign the imido protons of the coordinated imidazole groups in heme proteins.

• Bulletin of the Korean Chemical Society
• /
• v.23 no.12
• /
• pp.1790-1800
• /
• 2002

The DNA nucleosides(dA, dC, dG, dT)bound to gold nanoparticles (~13 nm) in aqueous solution has been studied as a probe by the SERS and their coordination structures have been proposed on the basis of them. According to UV-Visible absorption of gold nanoparticles after modifying with DNA nucleosides, the rates of absorption of dA, dC, and dG were much faster than that of dT as monitored by the aggregation kinetics at 700 nm. These data indicated that the nucleosides dA, dC, and dG had a higher affinity for the gold nanoparticles surface than nucleoside dT. As the result of SERS spectra, the binding modes of each of the nucleosides on gold nanoparticles have been assigned. A dA binds to gold nanoparticles via a N(7) nitrogen atom of the imidazole ring, which the C(6)-$NH_2$ group also participates in the coordination process. In the case of dC, it binds to the gold surface via a N(3) nitrogen atom of the pyrimidine ring with a partial contribution from the oxygen of C(2)=O group. A coordination of dG to the gold surfaces is also proposed. Although the dG has the two different nitrogens of a pyrimidine ring and the amino group, the N(1) nitrogen atom of a pyrimidine ring has a higher affinity after the hydrogen migrates to the amino group. Conversely, dT binds via the oxygen of the C(4)=O group of the pyrimidine ring. Accordingly, these data suggest that the nitrogen atom of the imidazole or the pyrimidine ring in the DNA nucleosides will bind more fast to the gold nanoparticles surfaces than the oxygen atom of the carbonyl group.