• Bulletin of the Korean Chemical Society
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• 제9권4호
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• pp.209-212
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• 1988

The hydrophobic interaction leading to the formation of ion-pair between $MB^+$ and $TPB^-$ was investigated spectroscopically by varying the medium with the addition of 1,A-dioxane or urea. Beyond 0.01 mole fraction of 1,A-dioxane in water or above 2.0M urea the ion-pair appeared to be completely dissociated into individual ions. The ion-pair was not observed in common organic solvents and the absorption maxima of $MB^+$ were correlated relatively well with the ${\pi}^{\ast}$-scale.

• Journal of Applied Biological Chemistry
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• 제42권3호
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• pp.125-129
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• 1999

The changes in gel characteristics of soy protein and succinylated soy protein due to various specific interaction-altering reagents which affect the formation and textural properties of gels, were studied. The reagents were added to 15% soy protein solutions prior to heat treatment. Succinylated soy protein formed harder gel without the addition of reagents. Hardly no gels were formed with urea, indicating that hydrogen bonds significantly contributed to the formation and hardness of the gel and the effects of urea on the hardness of succinylated soy protein gel were more significant. Disulfide bonds were important in the formation of hard gels whether they were succinylated or not, but the contributions of hydrophobic interactions to gel hardness were relatively insignificant. The hardness reducing effects of NaCl and NaSCN were more significant in succinylated soy protein gel. As such, electrostatic interactions were important for succinylated soy protein to form hard gel but not for unmodified soy protein.

• Bulletin of the Korean Chemical Society
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• 제23권8호
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• pp.1073-1077
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• 2002

Binding of dodecyl trimethylammonium bromide (DTAB) to human and bovine hemoglobin and globin samples has been investigated in 50 mM glycine buffer pH = 10, I = 0.0318 and 300 K by equilibrium dialysis and temperature scanning spectrophotometry techniques and method for calculation of average hydrophobicity. The binding data has been analyzed, in terms of binding capacity concept $({\theta})$, Hill coefficient (nH) and intrinsic Gibbs free energy of binding $({\Delta}Gbv).$ The results of binding data, melting point (Tm) and average hydrophobicity show that human hemoglobin has more structural stability than bovine hemoglobin sample. Moreover the results of binding data analysis represent the systems with two and one sets of binding sites for hemoglobin and globin, respectively. It seems that the destabilization of hemoglobin structure due to removal of heme group, is responsible of such behavior. The results indicating the removal of heme group from hemoglobin caused the depletion of first binding set as an electrostatic site upon interaction with DTAB and exposing the hydrophobic patches for protein.

• Archives of Pharmacal Research
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• 제10권2호
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• pp.69-74
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• 1987

The characteristics of zipeprol-$\beta$-cyclodextrin system were studied by circular dichroism, competitive UV method and dialysis method. In this experiment, binding constants by competitive UV method, circular dichroism and dialysis method were 155 M$^{-1}$ 187 M$\^{-1}$/($\pm$ 5%) and 315 $^{-1}$, repectively. It shows that zipeprol forms 1:1 compelx with $\beta$-cyclodextrin by circular dichroism and 1:2 by dialysis method. pH profile shows that binding force seems to be a hydrophobic interaction. It is suggested that benzene ring be accomodated in the cavity of $\beta$-cyclodextrin.

• Archives of Pharmacal Research
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• 제4권2호
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• pp.99-107
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• 1981

To investigate the protein binding characteristics of ibuprofenlysine, the effects of drub conentration, pH, ionic strength and protein concentration on the binding of drug to protein concentration on the binding of drug to protein were studied by fluorescence probe method. The conformational change of protein was investigated by circular dichroism (CD) measurement. As the concentration of drug increases, the association constant decreases. These may be due to complex formation of the probe and drug, or the interaction of the protein-probe complex and drug. The association constant for ibuprofenlysine increased with increasing protein concentration. These finding suggest a sharing of one ibuprofenlysine molecule by more than one protein molecule in the binding. The binding between ibuprofenlysine and protein was dependent on pH and ionic strength. It seems that both hydrophobic binding and some electrostatic forces are involved in the binding of ibuprofenlysing to protein.

• 한국자기공명학회논문지
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• 제9권2호
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• pp.155-162
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• 2005

The interaction of poly(ethylene glycol)(PEG) with cationic dodecyl trimethyl ammonium bromide (DTAB)micelle was studied with electron spin resonance (ESR) by determining line widths of the ESR spectra and coupling constant of nitrogen($A_N$). The degree of ESR line shape change such as line widths and coupling constant indicated that PEG mixes well with DTAB micelle due to a great hydrophobic interaction with surfactant alkyl chains. This suggests that the PEG can be used as non-ionic surfactant to disperse the exposed oil in the ocean.

• 한국자기공명학회논문지
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• 제1권1호
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• pp.59-70
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• 1997

The interaction of poly(ethylene glycol) (PEG) with cationic dodecyl trimethyl ammonium bromide (DTAB) micelle was studied with electron spin resonance (ESR) by determining line widths of ESR spectra and coupling constant of nitrogen(AN). The degree of ESR line shape change such as line widths and coupling constant indicated that PEG mixes well with DTAB micelle due to a great hydrophobic interaction with surfactant alkyl chains. This suggests that the PEG can be used as non-ionic surfactant to disperse the exposed oil in the ocean.

• Bulletin of the Korean Chemical Society
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• 제4권3호
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• pp.123-127
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• 1983

The crystal structure of metoclopramide, $C_14H_22ClN_3O_2$, has been determined by X-ray diffraction techniques using diffractometer data obtained by the ${\omega}-2{\theta}$ scan technique with Mo $K\alpha$ radiation from a crystal with space group symmetry $P{\overline{1}}$ and unit cell parameters a = 7.500(1), b = 8.707(2), c = 13.292(2) ${\AA}$; ${\alpha}$ = 101.70(2), ${\beta}$ = 81.20(2), and ${\gamma}$ = $114.90(l)^{\circ}$. The sructure was solved by direct methods and refined by full-matrix least-squares to a final R = 0.055 for the 1524 observed reflections. The bent overall-conformation of the molecule seems to be determined mainly by the bifurcated intramolecular hydrogen bond from the amide nitrogen atom to the methoxy oxygen and the amine nitrogen atoms. The crystal packing consists of the hydrogen bonds, ${\pi}-{\pi}$ interaction and hydrophobic interaction.

• Bulletin of the Korean Chemical Society
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• 제19권11호
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• pp.1194-1198
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• 1998

The density and the viscosity of aqueous PEO solutions are observed with the several concentrations of PEO at 20 ℃. The effects of urea on them are also observed. The apparent and the partial specific volumes of PEO are calculated from the density data, which result that the polymer-polymer interaction is dominating in the binary aqueous PEO solutions, while the polymer-solvent interaction is dominating in the ternary aqueous urea-PEO solutions. It is explained by the urea induced breakage of the structured water originated from the hydrophobic interactions and the binding of the urea to the PEO chain. The concentration dependence of relative viscosity and the density dependence of fluidity is also discussed with the concept of the polymersolvent and the polymer-polymer interactions of aqueous urea-PEO solutions.

• 상하수도학회지
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• 제28권4호
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• pp.419-429
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• 2014

Recent studies have been reported the presence of Endocrine Disrupting Compounds, Pharmaceuticals and Personal Care Products (EDC/PPCPs) in surface and wastewater, which could potentially affect to the complicate behavior in coupled presence of nano-colloid particles and surfactants (adsorption, dispersion, and partitioning). In this study, the adsorption of EDC/PPCPs by Single Walled Carbon Nanotubes (SWNTs) as a representative of nano-particles in cationic surfactant solutions were investigated. Hydrophobic interactions (${\pi}-{\pi}$ Electron Donor-Acceptor) have been reported as a potential adsorption mechanisms for EDC/PPCPs onto SWNTs. Generally, the adsorptive capacity of the relatively hydrophobic EDC/PPCPs onto SWNTs decreased in the presence of cationic surfactant (Cetyltrimethyl Ammonium Bromide, CTAB). This study revealed that the competitive adsorption occurred between CTAB cations and EDC/PPCPs by occupying the available SWNT surface (CTAB adsorption onto SWNTs shows five-regime and maximum adsorption capacity of 370.4 mg/g by applying the BET isotherm). The adsorption capacity of $17{\alpha}$-ethinyl estradiol (EE2) on SWNT showed the decrease of 48% in the presence of CTAB. However, the adsorbed naproxen (NAP) surely increased by forming hemimicelles and resulted in a favorable media formation for NAP partition to increase SWNTs adsorption capacity. The adsorbed NAP increased from 24 to 82.9 mg/g after the interaction of CTAB with NAP. The competitive adsorption for EDC/PPCPs onto SWNTs is likely to be a key factor in the presence of cationic surfactant, however, NAP adsorption showed a slight competition through $CH_3-CH_3$ interaction by forming hemimicelles on SWNT surface.