TY - JOUR
T1 - Processing Influence on Molecular Assembling and Structural Conformations in Silk Fibroin
T2 - Elucidation by Solid-State NMR
AU - Callone, Emanuela
AU - Dirè, Sandra
AU - Hu, Xiao
AU - Motta, Antonella
N1 - Publisher Copyright:
© 2016 American Chemical Society.
PY - 2016/5/9
Y1 - 2016/5/9
N2 - This study is devoted to the deep evaluation of processing-induced protein conformation changes by using silk fibroin fibers and their cast films stabilized by different methods as a model. The control of the hierarchical assembling of silk fibroin is the key for finely tuning the biological functions and physical-chemical properties of the final materials for applications in biomedical fields. However, previous methods usually only focused on the change of beta-sheet crystallinity in silk materials, which can not explain a lot of their specific prosperities generated from different processing methods. By using complementary solid-state NMR, together with FTIR and DSC techniques, we for the first time established the correlations between processing conditions and silk fibroin molecular configurations, and experimentally assess the presence and quantify the percentage of the asymmetric 3-fold helical conformation (Silk III) in silk materials, together with their well-known Silk I-like helix/coil dominated and Silk II beta-sheet dominated configurations. This work provides a roadmap for researchers to quantify the percentage of different silk structures by solid NMR, and further understand how silk molecular conformations (Silk I-like, II, III) can impact the properties and functions of different silk materials, that are broadly used today for different biomedical applications.
AB - This study is devoted to the deep evaluation of processing-induced protein conformation changes by using silk fibroin fibers and their cast films stabilized by different methods as a model. The control of the hierarchical assembling of silk fibroin is the key for finely tuning the biological functions and physical-chemical properties of the final materials for applications in biomedical fields. However, previous methods usually only focused on the change of beta-sheet crystallinity in silk materials, which can not explain a lot of their specific prosperities generated from different processing methods. By using complementary solid-state NMR, together with FTIR and DSC techniques, we for the first time established the correlations between processing conditions and silk fibroin molecular configurations, and experimentally assess the presence and quantify the percentage of the asymmetric 3-fold helical conformation (Silk III) in silk materials, together with their well-known Silk I-like helix/coil dominated and Silk II beta-sheet dominated configurations. This work provides a roadmap for researchers to quantify the percentage of different silk structures by solid NMR, and further understand how silk molecular conformations (Silk I-like, II, III) can impact the properties and functions of different silk materials, that are broadly used today for different biomedical applications.
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U2 - 10.1021/acsbiomaterials.5b00507
DO - 10.1021/acsbiomaterials.5b00507
M3 - Article
AN - SCOPUS:85001514080
VL - 2
SP - 758
EP - 767
JO - ACS Biomaterials Science and Engineering
JF - ACS Biomaterials Science and Engineering
SN - 2373-9878
IS - 5
ER -