Packing Structure of Antiparallel β-sheet Polyalanine Region in a Sequential Model Peptide of Dragline Silk Studied Using C Solid-State NMR and MD simulation.

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ID: 15159
2019
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Abstract
The packing structures of polyalanine regions, which are considered to be the reason for the extremely high strength of spider dragline silks, were studied using a series of sequential peptides: (Glu)GlyGlyLeuGlyGlyGlnGlyAlaGly(Ala)nGlyGlyAlaGlyGlnGlyGlyTyrGlyGly(Glu) (n = 3-8) using C solid-state NMR spectroscopy. The conformations of (Ala) in the freeze-dried peptides changed gradually with increasing n from random coils to α-helices with partial antiparallel β-sheet (AP-β) structures. Conversely, all the insolubilized peptides, n = 6-8 after low-pH treatment and n = 4-8 after formic acid/methanol treatment, formed AP-β structures with significant amounts of staggered packing arrangements. These results are different from previously obtained results for pure alanine oligopeptides, i.e., AP-β (Ala) formed rectangular packing for less than n = 6 but staggered packings for n ≥ 7. The C-labeled peptides were also used to confirm the staggered packing arrangements from NMR dynamics. Furthermore, MD simulation supported the observed results.
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asakura2019packingbiomacromolecules Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Asakura, Tetsuo;Nishimura, Akio;Aoki, Akihiro;Naito, Akira;
Journal Biomacromolecules
Year 2019
DOI
10.1021/acs.biomac.9b00969
URL
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