Location and conformation of amyloid β(25-35) peptide and its sequence-shuffled peptides within membranes: Implications for aggregation and toxicity in PC12 cells

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Title:	Location and conformation of amyloid β(25-35) peptide and its sequence-shuffled peptides within membranes: Implications for aggregation and toxicity in PC12 cells
Authors:	陳青諭;Tsai, Hui‐Hsu Gavin;Lee, Jian‐Bin;Shih, Yuan‐Ci;Wan, Lei;Shieh, Fa‐Kuen;Chen, Chin‐Yu
Contributors:	生醫理工學院生命科學系
Date:	2014-01-01
Issue Date:	2026-04-23 11:13:15 (UTC+8)
Publisher:	John Wiley and Sons Ltd;Wiley
Abstract:	摘要： AbstractExtracellular deposits of amyloid β (Aβ) aggregates in the brain is the hallmark of Alzheimer’s disease. We present the configurations (location and conformation) and the interfacial folding and membrane insertion mechanisms of Aβ fragments, wild‐type Aβ(25–35), Aβ(35–25), and a sequence‐shuffled peptide [Aβ(25–35)‐shuffled] from Aβ(25–35) within membranes by replica‐exchange molecular dynamics simulations. Although these peptides have the same amino acid composition, simulations show they have distinct locations and conformations within membranes. Moreover, our in vitro experiments show that these peptides have distinct neurotoxicities. We rationalize the distinct neurotoxicities of these peptides in terms of their simulated locations and conformations in membranes. This work provides another view that complements the general hydrophobicity–toxicity views, to better explain the neurotoxicity of Aβ peptides. 出版者： Wiley 出版日期： 2014-04-11 出處： ChemMedChem, 2014-04, Vol.9 (5), p.1002-1011 識別號： ISSN: 1860-7179 識別號： DOI: 10.1002/cmdc.201400062
Appears in Collections:	[Department of Life Science] journal & Dissertation

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