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  • Title: Lamellar Structure in Alanine-Glycine Copolypeptides Studied by Solid-State NMR Spectroscopy: A Model for the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form.
    Author: Asakura T, Aoki A, Komatsu K, Ito C, Suzuki I, Naito A, Kaji H.
    Journal: Biomacromolecules; 2020 Aug 10; 21(8):3102-3111. PubMed ID: 32603138.
    Abstract:
    Bombyx mori silk fibroin (SF) fibers with excellent mechanical properties have attracted widespread attention as new biomaterials. However, the structural details are still not conclusive. Here, we propose a lamellar structure for the crystalline domain of the SF fiber based on structural analyses of the Ala Cβ peaks in the 13C cross-polarization/magic angle spinning NMR spectra of (Ala-Gly)m (m = 9, 12, 15, and 25) and 13C selectively labeled (Ala-Gly)15 model peptides. Namely, three Ala Cβ peaks with relative intensities of 1:2:1 obtained by deconvolution were assigned to two kinds of β-sheet and a β-turn, which are interpreted as a lamellar structure formed by repetitive folding using β-turns every eighth amino acid, for which the basic structure is (Ala-Gly)4 in an antipolar arrangement. The dynamics and intermolecular arrangement were further studied using 13C solid-state spin-lattice relaxation time observations and the rotational echo double resonance experiments, respectively.
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