Earticle

초록

영어

Prion diseases are transmissible neurodegenerative disorders of protein conformation where the posttranslational modification of host-encoded prion protein PrPc yields a high -sheet content β modified protein PrPsc which further polymerizes into amyloid fibrils. PrP106-126 is the key region for initiating conformational changes that leads the conversion of PrPc to PrPsc.1) Molecules which can destabilize and defunctionalize such proteins can serve as a potential
tool in combating prion diseases. In microorganisms during stressed conditions, small stress molecules are formed to prevent protein denaturation and maintain protein stability and function.2) Hence they can prevent abnormal protein folding like amyloid formation. This work explores the effect of such small stress molecules on PrP106-126 amyloid formation. The characterization tools used for this study include turbidity, atomic force microscopy and cell viability assay. According to our results ectoine and mannosylglyceramide exhibited inhibitory
effects against prion peptide aggregation and toxicity to human neuroblastoma cells. Our findings conclude that small stress molecules could be potential inhibitors for prion diseases.

저자

• Mathumai Kanapathipillai [ Department of Chemical and Materials Engineering, Arizona State University ]
• Sook Hee Ku [ Department of Materials Science and Engineering, Korea Advanced Institute of Science and Technology ]
• Koyeli Girigoswami [ Department of Materials Science and Engineering, Korea Advanced Institute of Science and Technology ]
• Chan Beum Park [ Department of Chemical and Materials Engineering, Arizona State University, Department of Materials Science and Engineering, Korea Advanced Institute of Science and Technology ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576