Research Article
Safety Evaluation of Recombinant Bovine Lactoferrin as a Novel Biomaterial
Jiamiao Sun,
Sumin Zhang,
Yong Wang,
Jinchi Wei,
Yonghui Teng,
Binghua Quan,
Xiaoming Pang,
Honghong Deng,
Chiming Wei*
Issue:
Volume 10, Issue 1, March 2024
Pages:
1-8
Received:
1 February 2024
Accepted:
20 February 2024
Published:
7 March 2024
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.
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 f...
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