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02월 23일 15시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능
Assembly of Unstructured Protein Leading To Fibrillar Suprastructure Formation: α-Synuclein and Double-Concerted Fibrillation Model
2009년 2월 18일 15시 33분 56초
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목 15시 : 40분
Protein-Folding & Disease
서울대학교 화학생물공학부, Korea
Emergence of a large structure from its constituting small pieces has been one of the fundamental questions to be answered in a wide variety of areas including chemistry, biology, and even social science. Amyloid fibrils as a self-assembled product of soluble proteins are found in various neurodegenerative disorders and also recognized as high-performance protein nanomaterials with formidable strength. Elucidation of an underlying molecular mechanism of the amyloid fibril formation, therefore, is crucial not only to control the diseases but also to apply the protein fibrils for future nanobiotechnology. α-Synuclein is an amyloidogenic protein responsible for the Lewy body formation in Parkinson’s disease (PD). In the middle of a lag phase during the in vitro fibrillation of α-synuclein, discernable homogeneous granules made of 11 monomers in average were obtained. These oligomeric granular species of α-synuclein experienced almost instantaneous fibrillation following either the hexane-treatment or the 12-min single centrifugal membrane-filtration (Microcon YM-30) at 14,000 x g. The granular assembly leading to the drastically accelerated fibril formation has been demonstrated to be caused by both chemical and physical influences. Structural distortion of the preformed oligomeric structures is attributable for the suprastructure formation in which the oligomeric granular species act as a growing unit for the fibril formation. To parallel the prevailing notion of nucleation-dependent amyloidogenesis, we propose a double-concerted fibrillation model as one of mechanisms to explain the in vitro fibrillation of α-synuclein, in which two consecutive concerted interactions of the monomers and the subsequent oligomeric granules are hypothesized to be responsible for the eventual amyloid fibril formation. This model of the suprastructure formation, therefore, could contribute to various areas in science and technology in terms of offering not only practical evidence but also conceptualization of the large structure formation.
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