Influence of repeating sequence on structural and thermal stability of crystalline domain of bombyx mori silk fibroin

Biomedical applications of silk and its role for intervertebral disc repair

“…[45][46][47] A SF H-chain is designed as a natural block-copolymer with a repetitive core formed by 12 domains forming the crystalline region of SF interspersed with 11 less organized domains composed of a nonrepetitive primary sequence. 35,43 This block-copolymer arrangement of the H-chain guarantees the characteristic mechanical properties of SF. 48 The other protein constituting the silk cocoon is SS, a globular protein.…”

“…125 SF-based scaffolds also display high thermal stability, depending mainly on the primary and secondary structure. 35 Silk I and Silk II crystals melt at different temperatures, that is, 260-292 C and 286-350 C as a mean value, respectively. 126,127 Also, the processing technique and post-treatments influence the thermal stability of SF scaffolds.…”

“…Silks from silkworms and spiders have been widely studied for their use in tissue engineering and regenerative medicine 32–34 . Depending on the source, the biological and physicochemical properties change due to the different structural compositions 35–37 …”

“… 42–44 The primary structure of the H‐chain is a polypeptide that is mainly composed of glycine (43%–46%, G), alanine (30%, A), serine (12%, S), tyrosine (5.3%, Y) and other amino acids 45–47 . A SF H‐chain is designed as a natural block‐copolymer with a repetitive core formed by 12 domains forming the crystalline region of SF interspersed with 11 less organized domains composed of a nonrepetitive primary sequence 35,43 . This block‐copolymer arrangement of the H‐chain guarantees the characteristic mechanical properties of SF 48 …”

“… 32 , 33 , 34 Depending on the source, the biological and physicochemical properties change due to the different structural compositions. 35 , 36 , 37 …”