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Alpha-Synuclein Protects a (R/S)-Nonspecific Esterase from Archaeglobus Fulgidus

초록

영어

α-Synuclein, a main component of Lewy Bodies (LB), is involved in protein aggregation in the brain. α-Synuclein, a small acidic protein of 140 amino acids, is characterized by 11-residue repeats in the N-terminal and highly flexible C-terminal regions. Structurally, α-synuclein does not possess significant secondary structural content. Interestingly, in previous studies, it has been shown that α-synuclein can act as a protective molecule against stress conditions such as heat. In addition, α-synuclein could also help enzyme activity by suppressing protein aggregation under denaturing conditions like small heat shock proteins (sHSPs). α-synuclein seems to bind the exposed regions of protein folding intermediates which might protect the protein from aggregation and inactivation. We have investigated the function of α-synuclein using a thermophilic esterase from Archaeglobus fulgidus. This esterase is a monomeric enzyme that requires no cofactors for its activity and can be utilized for wide range of biotechnological applications. Our results indicate that α-synuclein and its specific peptides could protect this enzyme from thermal and organic solvent induced inactivation.

저자정보

  • Seung Bum Kim Department of Molecular Science and Technology, Ajou University
  • Mira Kang Department of Molecular Science and Technology, Ajou University
  • Yeon Woo Ryu Department of Molecular Science and Technology, Ajou University
  • T. Doohun Kim Department of Molecular Science and Technology, Ajou University

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