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.

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.