Structural convergence among diverse, toxic β-sheet ion channels

Hyunbum Jang, Fernando Teran Arce, Srinivasan Ramachandran, Ricardo Capone, Ratnesh Lal, Ruth Nussinov

Research output: Contribution to journalArticlepeer-review

60 Scopus citations


Recent studies show that an array of β-sheet peptides, including N-terminally truncated Aβ peptides (Aβ11-42/17-42), K3 (a β2-microglobulin fragment), and protegrin-1 (PG-1) peptides form ion channel-like structures and elicit single channel ion conductance when reconstituted in lipid bilayers and induce cell damage through cell calcium overload. Striking similarities are observed in the dimensions of these toxic channels irrespective of their amino acid sequences. However, the intriguing question of preferred channel sizes is still unresolved. Here, exploiting ssNMR-based, U-shaped, β-strand-turn-β-strand coordinates, we modeled truncated Aβ peptide (p3) channels with different sizes (12- to 36-mer). Molecular dynamics (MD) simulations show that optimal channel sizes of the ion channels presenting toxic ionic flux range between 16- and 24-mer. This observation is in good agreement with channel dimensions imaged by AFM for Aβ9-42, K3 fragment, and PG-1 channels and highlights the bilayer-supported preferred toxic β-channel sizes and organization, regardless of the peptide sequence.

Original languageEnglish (US)
Pages (from-to)9445-9451
Number of pages7
JournalJournal of Physical Chemistry B
Issue number29
StatePublished - Jul 29 2010
Externally publishedYes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry


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