Bulletin of the Korean Chemical Society

  • 제30권8호
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  • Pages.1845-1850
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  • 2009
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  • 0253-2964(pISSN)
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  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
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Dimerization of Fibril-forming Segments of α-Synuclein

  • 발행 : 2009.08.20
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초록

We have performed replica-exchange molecular dynamics (REMD) simulations on the dimer formation of fibrilforming segments of $\alpha$-Synuclein (residues 71 - 82) using implicit solvation models with two kinds of force fields- AMBER parm99SB and parm96. We observed spontaneous formation of dimers from the extensive simulations, demonstrating the self-aggregating and fibril forming properties of the peptides. Secondary structure profile and clustering analysis showed that dimers with antiparallel $\beta$-sheet conformations, stabilized by well-defined hydrogen boding, are major species corresponding to global free energy minimum. Parallel dimers with partial $\beta$-sheets are found to be off-pathway intermediates. The relative instability of the parallel arrangements is due to the repulsive interactions between bulky and polar side chains as well as weaker backbone hydrogen bonds.

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피인용 문헌

  1. Computational Study on Oligomer Formation of Fibril-forming Peptide of α-Synuclein vol.33, pp.3, 2012, https://doi.org/10.5012/bkcs.2012.33.3.848
  2. Besides Fibrillization: Putative Role of the Peptide Fragment 71–82 on the Structural and Assembly Behavior of α-Synuclein vol.53, pp.41, 2014, https://doi.org/10.1021/bi5008707
  3. Theoretical reconsideration on the hydrogen bonding and coordination interactions of chlorophyll a in aqueous solution vol.15, pp.3, 2011, https://doi.org/10.1142/s1088424611003148