Fine Structural Analysis of Degummed Fibroin Fibers Reveals Its Superior Mechanical Capabilities

被引:1
|
作者
Eliaz, D. [1 ,5 ]
Kellersztein, I. [2 ]
Miali, M. E. [1 ]
Benyamin, D. [3 ,4 ]
Brookstein, O. [1 ]
Daraio, C. [2 ]
Wagner, H. D. [1 ]
Raviv, U. [3 ]
Shimanovich, U. [1 ]
机构
[1] Weizmann Inst Sci, Dept Mol Chem & Mat Sci, IL-7610001 Rehovot, Israel
[2] CALTECH, Div Engn & Appl Sci, Pasadena, CA USA
[3] Hebrew Univ Jerusalem, Inst Chem, Edmond J Safra Campus, Givat Ram, Jerusalem, Israel
[4] Weizmann Inst Sci, Dept Phys Complex Syst, Rehovot, Israel
[5] SilkIt Ltd, Ness Ziona, Israel
关键词
Silk fibers; Protein self-assembly; beta-sheet conformation; Mechanical properties; Degumming; X-RAY-SCATTERING; D-PLUS SOFTWARE; SILK FIBROIN; BOMBYX-MORI; CHAIN; VARIABILITY; TRANSITION; HYDRATION; FEATURES; BEHAVIOR;
D O I
10.1002/cssc.202401148
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Bombyx mori silk fibroin fibers constitute a class of protein building blocks capable of functionalization and reprocessing into various material formats. The properties of these fibers are typically affected by the intense thermal treatments needed to remove the sericin gum coating layer. Additionally, their mechanical characteristics are often misinterpreted by assuming the asymmetrical cross-sectional area (CSA) as a perfect circle. The thermal treatments impact not only the mechanics of the degummed fibroin fibers, but also the structural configuration of the resolubilized protein, thereby limiting the performance of the resulting silk-based materials. To mitigate these limitations, we explored varying alkali conditions at low temperatures for surface treatment, effectively removing the sericin gum layer while preserving the molecular structure of the fibroin protein, thus, maintaining the hierarchical integrity of the exposed fibroin microfiber core. The precise determination of the initial CSA of the asymmetrical silk fibers led to a comprehensive analysis of their mechanical properties. Our findings indicate that the alkali surface treatment raised the Young ' s modulus and tensile strength, by increasing the extent of the fibers' crystallinity, by approximately 40 % and 50 %, respectively, without compromising their strain. Furthermore, we have shown that this treatment facilitated further production of high-purity soluble silk protein with rheological and self-assembly characteristics comparable to those of native silk feedstock, initially stored in the animal ' s silk gland. The developed approaches benefits both the development of silk-based materials with tailored properties and the proper mechanical characterization of asymmetrical fibrous biological materials made of natural building blocks.
引用
收藏
页数:13
相关论文
共 13 条
  • [1] Morphological and structural analysis of treated sisal fibers and their impact on mechanical properties in cementitious composites
    Bahja, B.
    Elouafi, A.
    Tizliouine, A.
    Omari, L. H.
    JOURNAL OF BUILDING ENGINEERING, 2021, 34
  • [2] The influence of structural and chemical parameters on mechanical properties of natural fibers: a statistical exploratory analysis
    Bekraoui, Nasr
    El Qoubaa, Zakaria
    Chouiyakh, Hajar
    Faqir, Mustapha
    Essadiqi, Elhachmi
    JOURNAL OF POLYMER ENGINEERING, 2022, 42 (05) : 385 - 394
  • [3] Guinea fowl eggshell structural analysis at different scales reveals how organic matrix induces microstructural shifts that enhance its mechanical properties
    Rodriguez-Navarro, A. B.
    Dominguez-Gasca, N.
    Athanasiadou, D.
    Le Roy, N.
    Gonzalez-Segura, A.
    Reznikov, N.
    Hincke, M. T.
    Mckee, M. D.
    Checa, A. G.
    Nys, Y.
    Gautron, J.
    ACTA BIOMATERIALIA, 2024, 178 : 244 - 256
  • [4] Structure Analysis and Its Correlation with Mechanical Properties of Microcellular Polyamide Composites Reinforced with Glass Fibers
    Szewczykowski, Piotr
    Sykutera, Dariusz
    Czyzewski, Piotr
    Cieszko, Mieczyslaw
    Szczepanski, Zbigniew
    Nowinka, Bartosz
    MATERIALS, 2023, 16 (23)
  • [5] Structural and Functional Analysis of Bacillus subtilis YisP Reveals a Role of Its Product in Biofilm Production
    Feng, Xinxin
    Hu, Yumei
    Zheng, Yingying
    Zhu, Wei
    Li, Kai
    Huang, Chun-Hsiang
    Ko, Tzu-Ping
    Ren, Feifei
    Chan, Hsiu-Chien
    Nega, Mulugeta
    Bogue, Shannon
    Lopez, Daniel
    Kolter, Roberto
    Goetz, Friedrich
    Guo, Rey-Ting
    Oldfield, Eric
    CHEMISTRY & BIOLOGY, 2014, 21 (11): : 1557 - 1563
  • [6] Enhancing biotextile applications with nanocomposite fibers: Molecular dynamics and interferometric analysis of the structural and mechanical properties of treated polypropylene
    El-Sayed, Nayera M.
    Ibrahim, Medhat A.
    El-Bakary, Mohammed A.
    POLYMER ENGINEERING AND SCIENCE, 2025, : 1988 - 2007
  • [7] A fine-scale analysis reveals microgeographic hotspots maximizing infection rate between a parasite and its fish host
    Mathieu-Begne, Eglantine
    Blanchet, Simon
    Rey, Olivier
    Scelsi, Orlane
    Poesy, Camille
    Marselli, Geoffrey
    Loot, Geraldine
    FUNCTIONAL ECOLOGY, 2022, 36 (02) : 380 - 391
  • [8] Ecocomposites Based on High-Impact Polystyrene (HIPS) and Amazon Acai (Euterpe oleracea) Fibers: Influence of NaOH Treatment on Its Structural, Thermal, and Mechanical Properties
    Silva, E. C.
    da Silva, A. F.
    Rodrigues, Y. da S.
    Correia Junior, D. S.
    de Oliveira, L. M.
    Biondo, M. M.
    Felix, P. H. C.
    Sales, H. B. E.
    Sanches, E. A.
    MECHANICS OF COMPOSITE MATERIALS, 2023, 59 (01) : 147 - 158
  • [9] Structural analysis of receptor-like kinase SOBIR1 reveals mechanisms that regulate its phosphorylation-dependent activation
    Wei, Xue
    Wang, Yulu
    Zhang, Su
    Gu, Tianyi
    Steinmetz, Gabryel
    Yu, Haiyan
    Guo, Guoguang
    Liu, Xin
    Fan, Shilong
    Wang, Fengzhong
    Gu, Yangnan
    Xin, Fengjiao
    PLANT COMMUNICATIONS, 2022, 3 (02)
  • [10] Structural analysis of alternate sigma factor ComX with RpoC, RpoB and its cognate CIN promoter reveals a distinctive promoter melting mechanism
    Kunthavai, P. C.
    Kannan, Muthu
    Ragunathan, Preethi
    JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2022, 40 (14) : 6272 - 6285