• Journal of the Korean Chemical Society
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• v.67 no.2
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• pp.81-88
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• 2023

The contribution of hydrophobic residues to the protein folding reaction was studied by using HubWA variant proteins with I and L to V mutation. Folding kinetics of all V variant proteins was observed to be satisfied by a three-state on-pathway mechanism, U ⇌ I ⇌ N, where U, I, and N represent unfolded, intermediate, and native state, respectively. Three-state folding reaction was quantitatively analyzed and the free energy of folding of each elementary reactions and overall folding reaction, ΔG^o_UI, ΔG^o_IN, and ΔG^o_UN, were obtained. From the ratio of free energy difference between the variant protein and HubWA, ΔΔG^o_UI/ΔΔG^o_UN (ΔΔG^o_UI = ΔG^o_UI (variant protein) - ΔG^o_UI (HubWA) and ΔΔG^o_UN = ΔG^o_UN (variant protein) - ΔG^o_UN(HubWA)), the contribution of hydrophobic residues to HubWA folding was analyzed. The residues which are located in the hydrophobic core between α-helix and β-sheet, I3, I13, L15, I30, L43, I61 and L67, showed ΔΔG^o_UI/ΔΔG^o_UN value of ~0.5 when each of these residues was mutated to V, indicating that these residues form relatively solid hydrophobic core in the intermediate state. Residues located at the end of secondary structures and loop, I23, L69 and I36 showed ΔΔG^o_UI/ΔΔG^o_UN value below 0.4 when each of these residues was mutated to V, indicating that the region containing these residues are loosely formed in the intermediate state. V17A, L50V and L56V showed fairly high ΔΔG^o_UI/ΔΔG^o_UN value of ~0.8. Since L50 and L56 are located in the region containing long loop (residue 46 to 62), it is suggested that the high ΔΔG^o_UI/ΔΔG^o_UN value of these residues prevents the formation of aggregate at the early stage of folding reaction.

• The Korean Journal of Physiology and Pharmacology
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• v.2 no.3
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• pp.385-393
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• 1998

Human neutrophil elastase (HNElastase, EC 3.4.21.37), a causative factor of inflammatory diseases, was purified by Ultrogel AcA54 gel filtration and CM-Sephadex ion exchange chromatography. HNElastase was inhibited by phenylbutazone in a concentration dependent manner up to 0.4 mM, but as the concentration increased, the inhibitory effect gradually diminished. Binding of phenylbutazone to the human neutrophil elastase caused strong Raman shifts at 200, 440, and 1194 $cm^{-1}$. The peak at 1194 $cm^{-1}$ might be evidence of the presence $of\;-N=N-{\Phi}$ radical. The core area of the elastase, according to the visual molecular model of human neutrophil elastase, was structurally stable. A deeply situated active center was at the core area surrounded by hydrophobic amino acids. Directly neighboring the active site was one positively charged atom and two atoms carrying a negative charge, which enabled the enzyme and the drug to form a strong interaction. Phenylbutazone may form a binding, similar to a key & lock system to the atoms carrying opposite charges near the active site of the enzyme molecule. Furthermore, the hydrophobicity of the surrounding amino acid near the active site seemed to enhance the binding strength of phenylbutazone. Binding of phenylbutazone near the active site may cause masking of the active site, preventing the substrate from approaching the active site and inhibiting elastase activity.

• Bulletin of the Korean Chemical Society
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• v.31 no.1
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• pp.52-58
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• 2010

Human histamine H1 receptor (HHR1) is a G protein-coupled receptor and a primary target for antiallergic therapy. Here, the ligand-based three-dimensional pharmacophore models were built from a set of known HHR1 inverse agonists using HypoGen module of CATALYST software. All ten generated pharmacophore models consist of five essential features: hydrogen bond acceptor, ring aromatic, positive ionizable and two hydrophobic functions. Best model had a correlation coefficient of 0.854 for training set compounds and it was validated with an external test set with a high correlation value of 0.925. Using this model Maybridge database containing 60,000 compounds was screened for potential leads. A rigorous screening for drug-like compounds unveiled RH01692 and SPB00834, two novel molecules for HHR1 with good CATALYST fit and estimated activity values. The new lead molecules were docked into the active site of constructed HHR1 homology model based on recently crystallized squid rhodopsin as template. Both the hit compounds were found to have critical interactions with Glu177, Phe432 and other important amino acids. The interpretations of this study may effectively be deployed in designing of novel HHR1 inverse agonists.

• Journal of the Korean Society of Clothing and Textiles
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• v.19 no.6
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• pp.946-954
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• 1995

The purpose of this study is to modify the hydrophobic property and dyeability of polyethylene terephthalate fiber. Methacrylic acid (2nA) was graftpolymerized with benzoyl peroxide (BPO) as initiator onto polyethylene terephthalate fabrics. The results were as follow; 1. Graft-polymerization exhibited maximum graft ratio at a temperature of 100"C. 2. The polymer was gradually grafted in great amount to the surface of MA-g-PET as graft ration increase; with the cross-section examination of MA-g-PET, it was discovered that graft-polymeriation had also taken place inside the textile core. 3. Dyes absorption of basic dyes and disperse dyes was improved as craft ratio increase; with resistance to laundering, the former showed grade 3-4 and the latter showed grade 5.de 5.

• Proceedings of the Polymer Society of Korea Conference
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• 2006.10a
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• pp.255-255
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• 2006

Polymeric nanoparticles are recognized as promising drug carriers [1]. Here, novel tri-block copolymers based on poly PPDO, PCL and PEG were synthesized and employed for the formulation of reproducible polymeric nanoparticles [2]. To estimate the feasibility of the polymer to form polymeric nanoparticles, nanoparticles were prepared by co-solvent evaporation technique. Polymerization and structural features of the polymer were analyzed by different physico-chemical techniques. Existence of hydrophobic domains as a core of nanoparticles was characterized by $^{1}H-NMR$ spectroscopy, and further confirmed by fluorescence technique using pyrene as probe.

• Proceedings of the Polymer Society of Korea Conference
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• 2006.10a
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• pp.249-249
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• 2006

We have prepared an amphiphilic wedge-coil molecule consisting of a hydrophobic wedge-like segment and a hydrophilic poly(ethylene oxide) (PEO) segment. The wedge-coil block molecule self-assembles into cylindrical nanofibers in both polar as well as nonpolar solvents. Remarkably, the resulting nanofibers, as solvent polarity change from water to n-hexane, change from highly flexible coil-like to stiff rod-like characteristics. This dynamic switching in the stiffness of the nanofibers in response to solvent polarity is attributed to the structural inversion of cylindrical core from bulky dendritic segments with amorphous nature to crystallizable linear PEO segments.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2010.03b
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• pp.40-40
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• 2010

CdSe nanocrystals (NCs) have been decorated on singlewalled carbon nanotubes (SWCNTs) by combining a method of chemically modified substrate along with gate-bias control. CdSe/ZnS core/shell quantum dots were negatively charged by adding mercaptoacetic acid (MAA). The silicon oxide substrate was decorated by octadecyltrichlorosilane (OTS) and converted to hydrophobic surface. The negatively charged CdSe NCs were adsorbed on the SWCNT surface by applying the negative gate bias. The selective adsorption of CdSe quantum dots on SWCNTs was confirmed by confocal laser scanning microscope. The measured photocurrent clearly demonstrates that CdSe NCs decorated SWCNT can be used for photodetector and solar cell that are operable over a wide range of wavelengths.

• Bulletin of the Korean Chemical Society
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• v.35 no.12
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• pp.3583-3589
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• 2014

This study evaluated a simple and useful route to the synthesis of mesoporous $TiO_2$ microcapsules with a hollow macro-core structure. A hydrophilic precursor sol containing the surfactants in the hydrophobic solvents was deposited on PMMA polymer surfaces modified by non-thermal plasma to produce mesoporous shells after calcination. The surface of the PMMA polymer spheres was coated with $NH_4F$ and CTAB to control the interfacial properties and promote the subsequent deposition of inorganic sols. These hollow type mesoporous $TiO_2$ microcapsules could be applied as an efficient substrate for the immobilization of DNA oligonucleotides.

• Proceedings of the Korea Crystallographic Association Conference
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• 2002.11a
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• pp.49-49
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• 2002

A strategy for the synthesis of more stable and large periodic mesoporous organo-silica materials has been developed for the 2D hexagonal mesoporous organosilica by the core-shell approach using nonionic PEO-PLGA-PEO triblock copolymer templates. The BET surface area of the solvent-extracted hexagonal mesoporous organosilica is estimated to be 1,016 ㎡/g and the pore volume, pore diameter, and wall thickness are 1.447 ㎤/g, 65 Å, and 43 Å, respectively. More hydrophobic PLGA block than the PPO block used for templates of mesoporous silica proves to be quite effective in confining the organosilicates within the PEO phase. Reaction temperature and acid concentration of an initial solution as well as the chemical nature of the bloc k copolymer templates also demonstrate to be important experimental parameters for ordered organosilica mesophase. Moreover, the mesoporous organosilicas prepared with the PEO-PLGA-PEO block templates maintain their structural integrity for up to 25 days in boiling water at 100℃. The mesoporous materials with large pores and high hydrothermal stability prepared in this study has a potential for many applications.

• Proceedings of the Korean Biophysical Society Conference
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• 1996.07a
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• pp.11-11
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• 1996

The three-dimensional structure of the carboxyl-terminal domain of the E.coli RNA polymerase $\alpha$ subunit, which is regarded as the contact site for transcription activator proteins and the promoter UP element, was determined by NMR spectroscopy. Its compact structure of four helices and two long arms enclosing its hydrophobic core shows a folding topology distinct from those of other DNA-binding proteins. (omitted)