| 학회 | 한국화학공학회 |
| 학술대회 | 2010년 가을 (10/21 ~ 10/22, 대전컨벤션센터) |
| 권호 | 16권 2호, p.1509 |
| 발표분야 | 생물화공 |
| 제목 | Thermodynamic analysis of biomolecular interactionsby using isothermal titration calorimetry (ITC) |
| 초록 | Usual function of α-lactalbumin (α-LA) is synthesizing lactose as a coenzyme, however, it can gain an unusual function of inducing apoptosis selectively for cancer cells. For that the α-LA is required to form a complex with oleic acid. There are extensive researches on the structural properties of this complex, but its thermodynamic mechanism is still unclear. In this work, we apply ITC analysis mainly to elucidate both the thermodynamic mechanism and the reaction stoichiometry underlying the complexation between sodium oleate (SO) and apo bovine α-LA (apo BLA). The SO-apo BLA complexation was governed by hydrophobic interaction meaning that it was driven by entropy change (ΔS). Also its stoichiometry was determined as ~12.0. In addition Ca2+ and ANS (8-anilino-1-naphthalene sulfonicacid) binding phenomena were analyzed by ITC. In contrast, the Ca2+ binding was driven by enthalpy change (ΔH) indicating an electrostatic interaction. Eventually this work will provide insight on how ITC analysis can contribute to understanding the thermodynamic mechanism and thus developing a thermodynamic criterion to set up the optimum process for universal anti-cancer agent. |
| 저자 | 김기형 1 , 이은규 2 , Ken. H. Mok 3 , 정우진 4 , 오병철 4 |
| 소속 | 1 한양대, 2 경원대, 3 Trinity College Dublin, 4 가천의과학대 |
| 키워드 | α-lactalbumin ; oleic acid ; tumor selective cytotoxicity ; ITC ; stoichiometry |
| VOD | VOD 보기 |
| 원문파일 | 초록 보기 |
