Platform

Technology

Ranpirnase, a ribonuclease (RNase), is a member of the superfamily of enzymes which catalyze the degradation of RNA, and mediate several essential biological activities, namely, regulation of cell proliferation, maturation, differentiation, and cell death. Therefore, they are ideal candidates for the development of therapeutics for life-threatening diseases (including Ebola and autoimmune diseases), that require anti-proliferative and apoptotic properties.

RNases are a superfamily of enzymes which catalyze the degradation of RNA. Ranpirnase overcomes the known challenges of targeting RNA for therapeutic purposes.

 

Strong Antiviral Effect
Ranpirnase anti-viral activity was greater than 98% of all compounds seen by 3rd party testing lab.

Safety Profile
Over 1,000 patients dosed in FDA studies for cancer. Drug is known to be safe and should accelerate approval pathway.

Ready Formulation
TamirBio topical anti-viral application uses a well-understood, proprietary transdermal delivery system.

Physical Properties
A highly stable, heat-resistant single-chain protein of 104 amino acids. Molecular weight of 12 kDa.

Secure Manufacturing
TamirBio owns large quantity of Rana pipiens eggs and previous oncologic activity means manufacturing understood.

Mechanism Of Action
The compound is derived from frog eggs and preferentially enters infected cells. By degrading RNA, ranpirnase halts protein synthesis, thus blocking viral replication. Ranpirnase is shown to target tRNA and premiRNA, and has a mechanism similar to Dicer cytoplasmic RNase III. In addition to blocking protein synthesis machinery, the compound has been shown to up-regulate genes involved in key cell functions, including transcription regulation, cell cycle, apotosis, as well as the immune and stress response.


Publications

Kiesgen S, Liebers N, Cremer M, Arnold U, et al. A fusogenic dengue virus-derived peptide enhances antitumor efficacy of an antibody-ribonuclease fusion protein targeting the EGF receptor. Protein Eng Des Sel. 2014. Oct;27(10):331-8

Youle RJ1, Wu YN, Mikulski SM, Shogen K, et al. RNase inhibition of human immunodeficiency virus infection of H9 cells. Proc Natl Acad Sci U S A. 1994 Jun 21;91(13):6012-6.

Squiquera L, Taxman DJ, Brendle SA, Torres R, Sulley J, Hodge T, Christensen N, Sidransky D., et al. Ranpirnase eradicates human papillomavirus in cultured cells and heals anogenital warts in a Phase I study. Antivir Ther. 2017 Jan 25. doi: 10.3851/IMP3133.

Vert A, Castro J, Ribó M, Benito A, Vilanova M., et al. Activating transcription factor 3 is crucial for antitumor activity and to strengthen the antiviral properties of Onconase. Oncotarget. 2016 Dec 27. doi: 10.18632/oncotarget.14302.

 

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