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RISS 인기검색어
- 검색키워드
- 저자 : 한임호 (검색결과 2 건)
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바이오센서에 사용되는 센서 칩의 표면에 단백질이나 다른 생물 고분자 리간드를 고정시키기 위해서 일반적으로 사용되는 방법은 먼저 긴 사슬로 된alkane thiol로 SAM(Self-assembled monolayer)을 형성하고 여기에 수용체와의 화학반응에 필요한 작용기를 도입하는 것이다. 그러나 SAM의 형성이나 작용기 도입과 같은 화학적인 방법들은 비교적 전문적인 기술이 필요하고 번거로워서 바이오센서를 널리 사용하지 못하도록 하는 제한 요인이 되고 있다. 따라서 본 연구의 목적은 리간드의 화학적 고정을 위한 작용기를 도입한 QCM(Quartz Crystal Microbalance) 센서 칩을 만들어 연구자들이 한 번에 리간드를 고정할 수 있도록 하는 것이다. 이를 위해 먼저 센서 칩의 gold surface위에 MUA[11-mercapto-1-undecanoic acid]와 MHL[6-mercapto-1-hexanol]을 섞어 SAM을 형성하고 SAM표면의 친수성, 이온화반응, 단백질들과의 상호작용 등을 분석하였다. 다음으로 아미노기 고정을 위해 EDC[N-ethyl-N′-(3-dimethylaminopropyl)carbodiimide]와 NHS[N-hydroxysuccinimide]를 차례대로 반응시킨 NHS 센서 칩을 만들었다. 그리고 NHS 센서 칩의 단백질과의 반응성을 조사하였다. Chemical coupling of biomolecules to a sensor surface is one of the most critical steps in the biosensor development. Common coupling method includes preparation of SAM (Self-assembled monolayer) with long chain alkane thiol and introduction of a chemical group for the conjugation of biomolecules. Such chemical manipulations, however, have been a barrier to the wide use of biosensor. Therefore, the purpose of this research is the preparation of QCM sensor surface for the instant coupling of biomolecules. As a first step, mixed SAMs with various composition of MUA (11-mercapto-1-undecanoic acid) and MHL (6-mercapto-1-hexanol) were prepared on the QCM gold electrode surface and their properties were analyzed including hydrophilicity and ionic character. The carboxyl group exposed on the SAM surface was activated through the reactions with EDC [N-ethyl-N′-(3-dimethylaminopropyl)carbodiimide] and NHS (N-hydroxysuccinimide). Finally, immunoglobulin G protein was conjugated by using the NHS group. The optimal reaction conditions for the surface activation and stability of the conjugated protein were investigated.
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인삼으로부터 유래된 Ginsenoside Re와 Ginsenoside Re/Leucine 혼합물의 열처리 후 생리활성효과
한임호 강릉원주대학교 대학원 2016 국내박사
Ginsenoside Re is a triol type triterpene glycoside and is abundantly present in ginseng berry. Ginsenoside Re can be transformed into less-polar ginsenosides, namely, Rg2, Rg6, and F4 by heat-processing. The products of heat-processed Ginsenoside Re inhibited phosphorylation of CDK2 at Thr160 by upregulation of p21 level, resulting in S phase arrest. The products of heat-processed Ginsenoside Re also activated Caspase-8, Caspase-9, and Caspase-3, followed by cleavage of PARP, a substrate of Caspase-3, in a dose-dependent manner. Concurrently, alteration of mitochondrial factors such as Bcl-2 and Bax was also observed. Moreover, pretreatment with Z-VAD-fmk abrogated Caspase-8, Caspase-9, and Caspase-3 activations by the products of heat-processed Ginsenoside Re. We further confirmed that the anticancer effects of the products of heat-processed Ginsenoside Re in AGS cells are mainly mediated via generation of less-polar Ginsenosides Rg6 and F4. The structural change of Ginsenoside and the generation of Maillard reaction products (MRPs) are important to the increase in the biological activities of Panax ginseng. This study was carried out to identify the renoprotective component of P. ginseng using the Maillard reaction model experiment with Ginsenoside Re and leucine. Ginsenoside Re was gradually converted into less-polar Ginsenosides Rg2, Rg6 and F4 by heat-processing, followed by separation of the glucosyl moiety at carbon-20. The free radical-scavenging activity of the Ginsenoside Re–Leucine mixture was increased by heat-processing. The improved free radical-scavenging activity by heat-processing was mediated by the generation of MRPs from the reaction of Glucose and Leucine. The cisplatin-induced LLC-PK1 renal cell damage was also significantly reduced by treatment with MRPs. Moreover, the heat-processed Glucose–Leucine mixture (major MRPs from the Ginsenoside Re–Leucine mixture) showed protective effects against cisplatin-induced oxidative renal damage in rats through the inhibition of Caspase-3 activation.
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