Earticle

초록

영어

Extremolytes are osmolytes accumulated by extremophiles as a response to external stress and are known to act as chemical chaperones by stabilizing cellular structures1). Extremolytes have been shown to prevent protein misfolding by stabilizing its structure and can reach high intracellular concentrations without interference in metabolism. ß-Amyloid peptide (Aß) is the major constituent of senile plaques, the key pathological feature of Alzheimer´s disease.
Aß is physiologically produced as a soluble form, but the aggregation of Aß monomers causes neurotoxicity. Ectoine, an extremolyte widespread in halophiles has been shown to interfere with the formation of amyloid aggregates in vitro and amyloid-induced cytotoxicity2,3). Using AFM and an assay based on thioflavin T fluorescence, we have tested synthetic ectoine analogs and other osmolytes for their ability to interfere with Aß amyloid formation in vitro. We show that a synthetic analog of ectoine with widened ring size interferes effectively with amyloid fibril formation. The results indicate the possibility of designing synthetic compounds as potential inhibitors of amyloid formation associated with neurodegenerative diseases.

저자

• Jungki Ryu [ Dept. of Materials Science and Engineering, Korea Advanced Institute of Science and Technology ]
• Chan Beum Park [ Dept. of Materials Science and Engineering, Korea Advanced Institute of Science and Technology ]
• Georg Lentzen [ bitop AG, Stockumer Str. 28, 58453 Witten, Germany ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576