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Location and Conformation of Amyloid β(25-35) Peptide and Its Sequence-Shuffled Peptides Within Membranes: Implications for Aggregation and Toxicity in PC12 Cells

Location and Conformation of Amyloid β(25-35) Peptide and Its Sequence-Shuffled Peptides Within Membranes: Implications for Aggregation and Toxicity in PC12 Cells

Hui-Hsu Gavin Tsai, Jian-Bin Lee, Yuan-Ci Shih, Lei Wan, Fa-Kuen Shieh, Chin-Yu Chen

ChemMedChem. 2014 May;9(5):1002-11.

PMID: 24729535

Abstract:

Extracellular 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP147740736	Amyloid β-Protein Fragment 35-25		147740-73-6	Price

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