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<p><i>Bombyx mori</i> silk fibroin and the antimicrobial peptide cecropin B are promising biomolecules for biomedical applications due to their unique and complementary properties. In this study, we successfully expressed recombinant silk fibroin (R. fib) alone and in fusion with cecropin B (R. fib–cec) in <i>Pichia pastoris</i>, with yields of 6&#xa0;mg/L for R. fib and 1.3&#xa0;mg/L for the R. fib–cec fusion protein. Characterization of the proteins through SDS-PAGE, Western blotting, and MALDI-TOF confirmed the successful expression and purity of the recombinant proteins. Notably, the fusion protein exhibited potent broad-spectrum antibacterial activity against Gram-negative <i>Escherichia coli</i> and Gram-positive <i>Staphylococcus aureus</i>, highlighting its potential as an antimicrobial agent. Furthermore, the R. fib and the R. fib–cec demonstrated significant protective effects against H<sub>2</sub>O<sub>2</sub> and UVB-induced oxidative damage in human adult dermal fibroblast cells. Pretreatment with R. fib and R. fib–cec significantly improved cell viability and morphology. R. fib and R. fib–cec increased viable cell numbers in H₂O₂-treated cells (61.8% and 83.5%, respectively) compared to the control (33%), and in UVB-irradiated cells (67.7% and 87.3%, respectively) compared to the control (38%). Both proteins also significantly reduced LDH release, a marker of cell damage. These results demonstrate that R. fib, especially R. fib–cec, protects against oxidative stress-induced cellular damage, promoting cell proliferation and reducing cytotoxicity. These findings highlight the multifunctionality of the silk–cecropin B fusion protein, making it a promising candidate for diverse biomedical applications, including antimicrobial therapies, skin protection, and wound healing.</p>

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Genetically engineered silk fibroin with antibacterial and antioxidant properties

  • 期刊论文

  • 发表日期：

    2025年4月17日

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  • Chitra Manoharan,
  • Dyna Susan Thomas,
  • Rasalkar Sandhya Yashwant,
  • Gourab Roy,
  • Vijayan Kunjupillai,
  • Rakesh Kumar Mishra,
  • Upendra Nongthomba,
  • Ravikumar Gopalapillai

摘要

Bombyx mori silk fibroin and the antimicrobial peptide cecropin B are promising biomolecules for biomedical applications due to their unique and complementary properties. In this study, we successfully expressed recombinant silk fibroin (R. fib) alone and in fusion with cecropin B (R. fib–cec) in Pichia pastoris, with yields of 6 mg/L for R. fib and 1.3 mg/L for the R. fib–cec fusion protein. Characterization of the proteins through SDS-PAGE, Western blotting, and MALDI-TOF confirmed the successful expression and purity of the recombinant proteins. Notably, the fusion protein exhibited potent broad-spectrum antibacterial activity against Gram-negative Escherichia coli and Gram-positive Staphylococcus aureus, highlighting its potential as an antimicrobial agent. Furthermore, the R. fib and the R. fib–cec demonstrated significant protective effects against H2O2 and UVB-induced oxidative damage in human adult dermal fibroblast cells. Pretreatment with R. fib and R. fib–cec significantly improved cell viability and morphology. R. fib and R. fib–cec increased viable cell numbers in H₂O₂-treated cells (61.8% and 83.5%, respectively) compared to the control (33%), and in UVB-irradiated cells (67.7% and 87.3%, respectively) compared to the control (38%). Both proteins also significantly reduced LDH release, a marker of cell damage. These results demonstrate that R. fib, especially R. fib–cec, protects against oxidative stress-induced cellular damage, promoting cell proliferation and reducing cytotoxicity. These findings highlight the multifunctionality of the silk–cecropin B fusion protein, making it a promising candidate for diverse biomedical applications, including antimicrobial therapies, skin protection, and wound healing.