Earticle

초록

영어

Transmissible spongiform encephalopathies, including bovine spongiform encephalopathy and human Creutzfeldt-Jakob disease, are fatal neurodegenerative disease. The protein-only hypothesis holds that prion proteins are the infectious agents of transmissible spongiform encephalopathies. Two molecular forms of the prion protein, the infectious form (PrPSc) and the normal cellular form (PrPC), are believed to differ only by their conformation. PrPSc has been found to differ from PrPC by infectivity, an increased β-sheet content, an increased resistance to proteinase K and an oligomeric state rather that a monomeric state. In the prion protein, there is only one intramolecular disulfide bond that is believed to be changed to intermolecular linkage during the conversion of cellular form of prion protein (PrPC) into scrapie form (PrPSc). Thus, transient disulfide reduction is required, in which process the structural transition is the aim of this study. Fluorescence quenching, circular dichroism and electron paramagnetic resonance spectroscopy assay show that a-helical structure of PrPC becomes unstructured when disulfide bond is reduced. This state was aggregation-prone in water phase but becomes stabilized in the
presence of membrane due to its membrane binding ability. Finally, the deposition of prion protein in the membrane destabilized membrane integrity.

저자

• Jae-Yoon Shin [ School of Bioresource Sciences, Sungkyunkwan University ]
• Dae-Hyuk Kweon [ School of Bioresource Sciences, Sungkyunkwan University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576