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Asakura, Tetsuo; Naito, Akira

Structural analyses of silk fibroins based on the structures of oligoalanine, and periodic oligopeptides of L‐alanine and glycine using x‐ray diffraction and 13C solid‐state NMR methods

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  • Media type: E-Article
  • Title: Structural analyses of silk fibroins based on the structures of oligoalanine, and periodic oligopeptides of L‐alanine and glycine using x‐ray diffraction and 13C solid‐state NMR methods
  • Contributor: Asakura, Tetsuo; Naito, Akira
  • imprint: Wiley, 2023
  • Published in: Journal of Applied Polymer Science
  • Language: English
  • DOI: 10.1002/app.54302
  • ISSN: 0021-8995; 1097-4628
  • Keywords: Materials Chemistry ; Polymers and Plastics ; Surfaces, Coatings and Films ; General Chemistry
  • Origination:
  • Footnote:
  • Description: <jats:title>Abstract</jats:title><jats:p>The structures of (A)<jats:sub>12</jats:sub>, (AAAG)<jats:sub>7</jats:sub>, (AAG)<jats:sub>10</jats:sub>, (AG)<jats:sub>15</jats:sub>, and (AGG)<jats:sub>10</jats:sub> were determined using x‐ray diffraction and <jats:sup>13</jats:sup>C sold‐state NMR methods after different solvent treatments to obtain knowledge about the structural changes of silk fibroins (SFs) from <jats:italic>Samia cynthia ricini</jats:italic> (<jats:italic>S.c.ricini</jats:italic>) and <jats:italic>Bombyx mori</jats:italic> (<jats:italic>B. mori</jats:italic>). Three solvent treatments were performed: precipitation from dialysis of LiSCN (LiSCN/Dialysis) or LiBr (LiBr/Dialysis) aqueous solutions, and drying from formic acid (FA) or trifluoroacetic acid (TFA) solutions. (AAAG)<jats:sub>7</jats:sub> and (AAG)<jats:sub>10</jats:sub> as models of <jats:italic>S.c.ricini</jats:italic> SF, formed antiparallel β‐sheet structure with staggered packing configuration and did not change after LiSCN/Dialysis or LiBr/Dialysis and FA treatments. (AGG)<jats:sub>10</jats:sub> formed 3<jats:sub>1</jats:sub> helix structure and did not change with these solvent treatments either. On the other hand, (AG)<jats:sub>15</jats:sub> as model of <jats:italic>B. mori</jats:italic> SF formed Silk I (type II β‐turn) structure after LiBr/Dialysis treatment and Silk II (lamellar packing) structure after FA treatment. Especially, <jats:italic>B. mori</jats:italic> SF seems useful for biomaterials.</jats:p>