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Glycerin-Induced Conformational Changes in Bombyx mori Silk Fibroin Film Monitored by super(13) C CP/MAS NMR and super(1) H DQMAS NMR

International journal of molecular sciences, 2016-09, Vol.17 (9), p.1517-1517 [Peer Reviewed Journal]

ISSN: 1422-0067 ;EISSN: 1422-0067 ;DOI: 10.3390/ijms17091517

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  • Title:
    Glycerin-Induced Conformational Changes in Bombyx mori Silk Fibroin Film Monitored by super(13) C CP/MAS NMR and super(1) H DQMAS NMR
  • Author: Asakura, Tetsuo ; Endo, Masanori ; Hirayama, Misaki ; Arai, Hiroki ; Aoki, Akihiro ; Tasei, Yugo
  • Subjects: Bombyx mori
  • Is Part Of: International journal of molecular sciences, 2016-09, Vol.17 (9), p.1517-1517
  • Description: In order to improve the stiff and brittle characteristics of pure Bombyx mori(B. mori) silk fibroin (SF) film in the dry state, glycerin (Glyc) has been used as a plasticizer. However, there have been very limited studies on the structural characterization of the Glyc-blended SF film. In this study, super(13) C Cross Polarization/Magic Angle Spinning nuclear magnetic resonance (CP/MAS NMR) was used to monitor the conformational changes in the films by changing the Glyc concentration. The presence of only 5 wt % Glyc in the film induced a significant conformational change in SF where Silk I* (repeated type II beta -turn and no alpha -helix) newly appeared. Upon further increase in Glyc concentration, the percentage of Silk I* increased linearly up to 9 wt % Glyc and then tended to be almost constant (30%). This value (30%) was the same as the fraction of Ala residue within the Silk I* form out of all Ala residues of SF present in B. mori mature silkworm. The super(1) H DQMAS NMR spectra of Glyc-blended SF films confirmed the appearance of Silk I* in the Glyc-blended SF film. A structural model of Glyc-SF complex including the Silk I* form was proposed with the guidance of the Molecular Dynamics (MD) simulation using super(1) H- super(1) H distance constraints obtained from the super(1) H Double-Quantum Magic Angle Spinning (DQMAS) NMR spectra.
  • Language: English
  • Identifier: ISSN: 1422-0067
    EISSN: 1422-0067
    DOI: 10.3390/ijms17091517
  • Source: PubMed Central
    ProQuest Central
    DOAJ Directory of Open Access Journals
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