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Safety Evaluation of Recombinant Bovine Lactoferrin as a Novel Biomaterial

Received: 1 February 2024     Accepted: 20 February 2024     Published: 7 March 2024
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Abstract

This study introduces the physical principles and safety evaluation of recombinant bovine lactoferrin (fusion factor) as an innovative biomaterial. Fusion factor is a recombinant lactoferrin expressed by fusing lactoferrin, which has natural biological defense function, with other peptide segments through sequence optimization. It is named fusion factor. Its molecular weight is about 36kDa, which is much greater than the 1kDa molecular weight limit of macromolecular transdermal absorption, so it is not absorbed when used externally on the epithelial mucosa. The lactoferrin based biological defense functional peptide segment in the fusion factor can neutralize the virus by binding to viral protein nucleic acid through the physical action of charge adsorption, and can also compete with cell receptors to inhibit virus infection in cells. The molar ratio of the transmembrane peptide (Pep-1) fragment to the carrier protein is 1:1, so only the transport protein is anchored to the cell surface, forming a physical isolation protein protective wall against viruses and bacteria, without penetrating the cell or damaging the cell membrane. The fusion factor and its derived vaginal bacteria blocking gel have no significant toxicity, sensitization, anaphylaxis or delayed hypersensitivity in vitro cell experiments, in vivo animal experiments and clinical observation tests, and have no side effects with highly safety.

Published in International Journal of Biomedical Engineering and Clinical Science (Volume 10, Issue 1)
DOI 10.11648/j.ijbecs.20241001.11
Page(s) 1-8
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Recombinant Bovine Lactoferrin, Fusion Factor, Biological Defense, Physical Effects, Security

References
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Cite This Article
  • APA Style

    Sun, J., Zhang, S., Wang, Y., Wei, J., Teng, Y., et al. (2024). Safety Evaluation of Recombinant Bovine Lactoferrin as a Novel Biomaterial. International Journal of Biomedical Engineering and Clinical Science, 10(1), 1-8. https://doi.org/10.11648/j.ijbecs.20241001.11

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    ACS Style

    Sun, J.; Zhang, S.; Wang, Y.; Wei, J.; Teng, Y., et al. Safety Evaluation of Recombinant Bovine Lactoferrin as a Novel Biomaterial. Int. J. Biomed. Eng. Clin. Sci. 2024, 10(1), 1-8. doi: 10.11648/j.ijbecs.20241001.11

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    AMA Style

    Sun J, Zhang S, Wang Y, Wei J, Teng Y, et al. Safety Evaluation of Recombinant Bovine Lactoferrin as a Novel Biomaterial. Int J Biomed Eng Clin Sci. 2024;10(1):1-8. doi: 10.11648/j.ijbecs.20241001.11

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  • @article{10.11648/j.ijbecs.20241001.11,
      author = {Jiamiao Sun and Sumin Zhang and Yong Wang and Jinchi Wei and Yonghui Teng and Binghua Quan and Xiaoming Pang and Honghong Deng and Chiming Wei},
      title = {Safety Evaluation of Recombinant Bovine Lactoferrin as a Novel Biomaterial},
      journal = {International Journal of Biomedical Engineering and Clinical Science},
      volume = {10},
      number = {1},
      pages = {1-8},
      doi = {10.11648/j.ijbecs.20241001.11},
      url = {https://doi.org/10.11648/j.ijbecs.20241001.11},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijbecs.20241001.11},
      abstract = {This study introduces the physical principles and safety evaluation of recombinant bovine lactoferrin (fusion factor) as an innovative biomaterial. Fusion factor is a recombinant lactoferrin expressed by fusing lactoferrin, which has natural biological defense function, with other peptide segments through sequence optimization. It is named fusion factor. Its molecular weight is about 36kDa, which is much greater than the 1kDa molecular weight limit of macromolecular transdermal absorption, so it is not absorbed when used externally on the epithelial mucosa. The lactoferrin based biological defense functional peptide segment in the fusion factor can neutralize the virus by binding to viral protein nucleic acid through the physical action of charge adsorption, and can also compete with cell receptors to inhibit virus infection in cells. The molar ratio of the transmembrane peptide (Pep-1) fragment to the carrier protein is 1:1, so only the transport protein is anchored to the cell surface, forming a physical isolation protein protective wall against viruses and bacteria, without penetrating the cell or damaging the cell membrane. The fusion factor and its derived vaginal bacteria blocking gel have no significant toxicity, sensitization, anaphylaxis or delayed hypersensitivity in vitro cell experiments, in vivo animal experiments and clinical observation tests, and have no side effects with highly safety.
    },
     year = {2024}
    }
    

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    AU  - Jiamiao Sun
    AU  - Sumin Zhang
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    JF  - International Journal of Biomedical Engineering and Clinical Science
    JO  - International Journal of Biomedical Engineering and Clinical Science
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    AB  - This study introduces the physical principles and safety evaluation of recombinant bovine lactoferrin (fusion factor) as an innovative biomaterial. Fusion factor is a recombinant lactoferrin expressed by fusing lactoferrin, which has natural biological defense function, with other peptide segments through sequence optimization. It is named fusion factor. Its molecular weight is about 36kDa, which is much greater than the 1kDa molecular weight limit of macromolecular transdermal absorption, so it is not absorbed when used externally on the epithelial mucosa. The lactoferrin based biological defense functional peptide segment in the fusion factor can neutralize the virus by binding to viral protein nucleic acid through the physical action of charge adsorption, and can also compete with cell receptors to inhibit virus infection in cells. The molar ratio of the transmembrane peptide (Pep-1) fragment to the carrier protein is 1:1, so only the transport protein is anchored to the cell surface, forming a physical isolation protein protective wall against viruses and bacteria, without penetrating the cell or damaging the cell membrane. The fusion factor and its derived vaginal bacteria blocking gel have no significant toxicity, sensitization, anaphylaxis or delayed hypersensitivity in vitro cell experiments, in vivo animal experiments and clinical observation tests, and have no side effects with highly safety.
    
    VL  - 10
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Author Information
  • Department of Infectious Diseases, Chinese Academy of Biomedical Sciences, Hong Kong, China

  • Department of Infectious Diseases, Chinese Academy of Biomedical Sciences, Hong Kong, China

  • Department of Infectious Diseases, Chinese Academy of Biomedical Sciences, Hong Kong, China

  • Department of Infectious Diseases, Chinese Academy of Biomedical Sciences, Hong Kong, China; Department of Biomedical Engineering, Johns Hopkins University, Baltimore, USA

  • Department of Infectious Diseases, Chinese Academy of Biomedical Sciences, Hong Kong, China

  • Department of Infectious Diseases, Chinese Academy of Biomedical Sciences, Hong Kong, China

  • Department of Infectious Diseases, Chinese Academy of Biomedical Sciences, Hong Kong, China

  • Department of Infectious Diseases, Chinese Academy of Biomedical Sciences, Hong Kong, China

  • Department of Infectious Diseases, Chinese Academy of Biomedical Sciences, Hong Kong, China; Department of Nano Medicine, American Nanomedicine Institute, Baltimore, USA

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