Mechanisms of Membrane Pore Formation by Amyloidogenic Peptides in Amyotrophic Lateral Sclerosis

Charles H Chen, Ayesha Khan, Joseph Jen-Tse Huang, Martin B Ulmschneider

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

Using unbiased atomic-detailed molecular dynamics simulations, the C-terminal fragments of TDP-43 are observed to aggregate and form disordered-toroidal pores in a lipid bilayer. Cytotoxicity of TDP-43 may be inferred from the observation that the membrane pores catalyze lipid flip-flop between bilayer leaflets and conduct water at high rates.

Original languageEnglish
Pages (from-to)9958-9961
Number of pages4
JournalCHEMISTRY
Volume22
Issue number29
DOIs
Publication statusPublished - 11 Jul 2016

Keywords

  • Amyotrophic Lateral Sclerosis/metabolism
  • DNA-Binding Proteins/chemistry
  • Lipid Bilayers/chemistry
  • Membrane Proteins/chemistry
  • Molecular Dynamics Simulation
  • Peptides/chemistry
  • Water/chemistry

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