Instantaneous Amyloid Fibril Formation of -Synuclein from the Oligomeric Granular Structures in the Presence of Hexane

¹ Seoul National University

^* To whom correspondence should be addressed. E-mail: srpaik{at}snu.ac.kr.

Submitted on April 10, 2008
Revised on April 25, 2008
Accepted on 2 May 2008

	Abstract

Amyloid fibrils found in various neurodegenerative disorders are also recognized as high-performance protein nanomaterials with a formidable rigidity. Elucidation of an underlying molecular mechanism of the amyloid fibril formation is crucial not only to develop controlling strategy toward the diseases, but also to apply the protein fibrils for future nanobiotechnology. -Synuclein is an amyloidogenic protein responsible for the radiating filament formation within Lewy bodies of Parkinson's disease (PD). The amyloid fibril formation of -synuclein has been demonstrated to be induced from the oligomeric granular species of the protein acting as a growing unit by experiencing structural rearrangement within the preformed oligomeric structures in the presence of an organic solvent of hexane. This granule-based concerted amyloid fibril formation model would parallel the prevalent notion of nucleation-dependent fibrillation mechanism in the area of amyloidosis.

Key Words: Parkinson's disease, alpha-synuclein, amyloid fibril formation, granular assembly, hexane, protein nanofibrils