• Macromolecular Research
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• 제11권4호
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• pp.283-290
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• 2003

Organic drugs including aspirin, omeprazole, and naproxen with three different levels of octanol/water partition coefficient were examined for their release behavior from the amphiphilic PCL-b-PEO-b-PCL (PCEC) matrix. Scanning electron micrograph (SEM) of PCEC illustrated a well defined two-phase morphology consisted of dispersed poly(ethylene oxide) (PEO) domain and continuous polycaprolactone (PCL) phase. Differential scanning calorimetry (DSC) and X-ray diffractometry (XRD) experiments veri tied that three model drugs are dissolved as a molecular dispersion in PCEC matrix. The release of hydrophilic aspirin closely followed the water absorption profile of the matrix indicating that its major fraction is present in PEO domain. However, substantial amount of aspirin present in less hydrophilic region displayed discontinuous biphasic release pattern. In the case of omeprazole with intermediate hydrophobicity consistent release behavior was observed for a period of 24 hrs after the rapid liberation of ca. 10% of the drug presumably partitioned in PEO phase. It was ascribed to the fact that the progressive hydration of PCEC matrix gradually increased the chance of drug/water exposure to compensate the exhaustion of device. Naproxen with the highest octanol/water distribution coefficient among three model drugs exhibited a limited release of 35% for 24 hrs. Finally, hydroxypropyl methylcellulose phthalate (HPMCP)/PCEC blend matrix demonstrated an accelerated and quantitative release of hydrophobic naproxen by generating high porosity and thereby expanding polymer/water interface.

• Journal of Plant Biology
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• 제38권4호
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• pp.359-364
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• 1995

As the first step to elucidate the relationship between the structure and function of CTP:phosphocholine cytidylyltransferase (EC 2.7.7.15) in plants, the partial nucleotide sequence of soybean cytidylyltransferase cDNA was determined using a polymerase chain reaction (PCR). Degenerate oligonucleotide primers were synthesized from the conserved region revealed from the rat and yeast cytidylyltransferase DNA sequences. The catalytic domain region showed 78 and 76% homology with the rat and yeast amino acid sequences, respectivly. The hydropathy profile indicated that the C-terminal non-catalytic portion of the protein was very hydrophilic, and in the region between the catalytic domain and the C-terminal region, there was a large amphipathic $\alpha$-helical domain that was believed to bind the membrane surface in the active formation. There are 7 potential sites for phosphorylation by protein kinase C and 4 potential sites for phosphorylation by Ca2+/calmodulin kinase within the determined sequence.

• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 1995년도 춘계학술대회
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• pp.81-81
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• 1995

It is well known that Src Homology 2(SH2) domain in many intracellular signal transduction proteins is very important. The domain has about 100 amino acid residues and bind phosphotyrosine-containing peptide with high affinity and specificity. Lck SH2 domain is a Src-like, lymphocyte-specific tyrosine kinase. An 11-residue phosphopeptide derived from the hamster polvoma middle-T antigen, EPQp YEEIPIYL, binds with an 1 nM dissociation constant to Lck SH2 domain. And it is known that the phosphotyrosine and isoleucine residues of the peptide are tightly bound by two well-defined pockets on Lck SH2 domain's surface. To investigate the conformational changes during complexation of SH2 domain with phosphopeptide we have performed the molecular dynamics simulation for Lck SH2 domain with peptide and peptide-free form at look in aqueous solution. More than 3000 water molecules were incorporated to solvate Lck SH2 domain and peptide. Periodic boundary condition has been applied in molecular dynamics simulation. Data analysis with the results of that simulation shows that the phosphopeptide makes primary interaction with the Lck SH2 domain at six central residues, The comparison of the complexed and uncomplexed SH2 domain structures in solution has revealed only relatively small change. But the hydrophilic and hydrophobic pockets in the protein surface show the conformational changes in spite of the small structural difference between the complex and peptide-free forms.

• Parasites, Hosts and Diseases
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• 제44권3호
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• pp.251-254
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• 2006

Monoclonal antibody (mAb) Tg786 against Toxoplasma gondii has been found to detect a 42-kDa rhoptry protein (ROP6) which showed protease activity and host cell binding characteristics after secretion. Using the mAb, a colony containing a 3'-UTR was probed in a T. gondii cDNA expression library. A full length cDNA sequence of the rhoptry protein was completed after 5'-RACE, which consisted of 1,908 bp with a 1,443 bp ORF. The deduced amino acid sequence of ROP6 consisted of a polypeptide of 480 amino acids without significant homology to any other known proteins. This sequence contains an amino terminal stop transfer sequence downstream of a short neutral sequence, hydrophilic middle sequence, and hydrophobic carboxy terminus. It is suggested that the ROP6 is inserted into the rhoptry membrane with both N- and C-termini.

• International Journal of Industrial Entomology and Biomaterials
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• 제10권2호
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• pp.125-129
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• 2005

Ribosome-associated membrane protein 4 (RAMP4) is a membrane protein that exposes its N-terminal hydrophilic portion on the cytoplasmic side and spans the membrane close to the C-terminal end. RAMP4 has previously been reported to belong to the set of proteins that remains associated with membrane-bound ribosomes, and controls the glycosylation of major histocompatbility complex class II-associated invariant chain. RAMP4 also may be relative to the stabilization of membrane proteins in response to stress, with other components of translocon, and molecular chaperons in ER. Application of 5'-RACE technique with specially designed primer, we cloned a 715 bp cDNA fragment which contains a 195 bp ORF, termed RAMP4. The deduced protein has 64 amino acid residues and contains a putative transmembrane-spanning domain at the COOH terminus.

• 대한의용생체공학회:의공학회지
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• 제15권1호
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• pp.51-56
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• 1994

Protein adsorption on the polyurethane surface was modelled by a modified random sequential adsorption(RSA) process. In this model, polyurethane surface was modelled as a mixed domain of hydrophobic and hydrophilic parts which was implemented by a 2 dimensional $150{\times}150$ lattice in the computer. Protein adsorption was simulated using a small box which represents a particle of the protein, and polyurethane lattice by considering their hydrophobic interaction. In order to validate the model, we perfonned fibrinogen adsorption on polyurethane surface. Isotherms of the adsorbed protein were calculated and compared to the experimental data. The protein adsorption on the polyurethane surface could be well described using this computer model.

• 통합자연과학논문집
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• 제5권3호
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• pp.190-194
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• 2012

Human P-gp is one of the protein responsible for the multidrug resistance (MDR) develpment. MDR is a major cause of the cancer chemotherapy. In this paper, we performed homology modeling, docking study of papayriferic acid into the P-gp nucleotide binding domain (NBD2). For human P-gp, X-ray crystal structure is not known yet. We developed homology model for human NBD2 using HlyB ABC transporter structure (PDB code: 1XEF, resolution 2.5 ${\AA}$). Docking study was performed using Autodock. Docking result was analyzed, which shows that ligand docks into steroid binding site and interacts through hydrophobic and hydrophilic interactions.

• Molecules and Cells
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• 제26권2호
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• pp.140-145
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• 2008

Expression of olive flounder hepcidin I (HepI) fused with truncated OmpA signal peptides ($OmpASP_{tr}$) as directional signals does not produce soluble fusion proteins. However, by inserting amino acid segments (xxx) varying in pI and hydrophobicity/hydrophilicity into a leader sequence containing a truncated OmpASP ($OmpASP_{tr}$) and a factor Xa cleavage site (Xa) [$OmpASP_{tr}{\mid}(xxx){\mid}Xa$], we were able in some cases to express soluble recombinant HepI. Soluble expression of the recombinant protein strongly correlated with (xxx) insertions of high pI and hydrophilicity. Therefore, we modified the $OmpASP_{tr}{\mid}(xxx){\mid}Xa$ sequence by inserting Arg and Lys into (xxx) to increase the hydrophilicity of the signal peptide region. These modifications enhanced the expression of soluble recombinant HepI. Hydropathic profile analysis of the $OmpASP_{tr}{\mid}(xxx){\mid}Xa$ HepI fusion proteins revealed that the transmembrane-like domains derived from the $OmpASP_{tr}{\mid}(xxx){\mid}Xa$ sequence were larger than the internal positively charged domain native to HepI. It should therefore be possible to overcome the obstacle of internal positively charged domains to obtain soluble expression of recombinant proteins by monitoring the hydrophilicity and hydropathic profile of the signal peptide region using a computer program.

• 폴리머
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• 제29권1호
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• pp.1-7
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• 2005

상호 침투하는 고분자 가교구조(IPN)는 가교 고분자의 블렌드라고 볼 수 있다. IPN의 큰 특징 중의 하나는 IPN 합성 중 모폴로지의 조절이 가능하다는 점으로 반응속도와 상 분리 속도의 상대적인 크기에 따라 모폴로지의 조절이 가능하고 따라서 나노미터 크기의 분산상도 얻을 수 있고 상호연속 상(co-continuous phase)도 얻을 수 있다. 또 하나의 중요한 특징은 IPN 구조에 존재하는 가교구조 사이의 물리적 얽힘때문에 한번 형성된 모폴로지는 주위 환경에 관계없이 변하지 않는다는 점이다. 친수성 폴리우레탄과 소수성 폴리스티렌의 결합을 IPN 형태로 하면 표면에 친수성과 소수성 도메인이 공존하게 되고 이러한 표면이 우수한 혈액 적합성을 보인다. IPN 합성시 반응온도, 반응압력, 가교밀도 등을 변화시켜 소수성 폴리스티렌 도메인의 크기를 변화시키고 이에 따른 혈액 적합성의 변화를 연구하였다.

• Bulletin of the Korean Chemical Society
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• 제34권12호
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• pp.3665-3670
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• 2013

The R3V6 peptide includes a hydrophilic arginine stretch and a hydrophobic valine stretch. In previous studies, the R3V6 peptide was evaluated as a gene carrier and was found to have low cytotoxicity. However, the transfection efficiency of R3V6 was lower than that of poly-L-lysine (PLL) in N2A neuroblastoma cells. In this study, the transfection efficiency of R3V6 was improved in combination with high mobility group box 1A domain (HMGA). HMGA is originated from the nuclear protein and has many positively-charged amino acids. Therefore, HMGA binds to DNA via charge interaction. In addition, HMGA has a nuclear localization signal peptide and may increase the delivery efficiency of DNA into the nucleus. The ternary complex with HMGA, R3V6, and DNA was prepared and evaluated as a gene carrier. First, the HMGA/DNA complex was prepared with a negative surface charge. Then, R3V6 was added to the complex to coat the negative charges of the HMGA/DNA complex, forming the ternary complex of HMGA, R3V6, and DNA. A physical characterization study showed that the ternary complex was more stable than the PLL/DNA complex. The HMGA/R3V6/DNA complex had a higher transfection efficiency than the PLL/DNA, HMGA/DNA, or R3V6/DNA complexes in N2A cells. Furthermore, the HMGA/R3V6/DNA complex was not toxic to cells. Therefore, the HMGA/R3V6/DNA complex may be a useful gene delivery carrier.