|
Categories |
Peptide/Protein, Inflammation, Autoimmunity, Diabetes |
|
Development Stage |
Feasibility demonstrated in mouse models of both type 1 and type 2 diabetes (abbreviated T1D and T2D, respectively) |
|
Patent Status |
Provisional Patent application was submitted |
|
Market |
The disease is epidemic: 285 million patients in 2010, extrapolating to 440 million in 2030. Except insulin therapy , an efficient universal therapy does practically not exist |
Our Innovation
RHAMM peptides, that include the functional pathological domain of mouse RHAMM protein (which is hyaluronic acid binding motifs) display substantial anti-diabetic activity in both T1D (NOD mice) and T2D (db/db mice and high fat diet mice) experimental models, even when injected after the disease onset (Fig and 2,respectively). Efficacy of the peptide was proved in 7 different large scale experiences (4 related to T1D and 3 related to T2D) and injection protocol was established. Several diabetic parameters were analysed (e.g., blood glucose, blood insulin, glucose tolerance, insulin tolerance, urine albumin etc) , all of them support the major conclusion, indicated above. In vitro experiments show that the RHAMM peptides are not toxic and that RHAMM peptide protect insulin-secreting β cells from apoptosis, a fact which may explain the mechanism underlies the anti-diabetic effect of the peptide. In Fig 1 and Fig 2 RHAMM-50 peptide is described, which is designated also RHAMM-P1.
Highlights
-
RHAMM protein is expressed mostly in chronic inflammatory cells and cancer cells, and very rarely in adult normal cells (an exception is wound healing). Therefore, RHAMM targeting by the peptides should not affect innocent cells, engage in physiological functions.
-
The parental RHAMM protein includes oncogenic sequence, which is not included in the RHAMM peptides. On the other hand, parental RHAMM protein and the RHAMM peptides share the functional domain binding motifs. Therefore, the peptides can potentially block not only chronic inflammation, but also the malignant activity of parental RHAMM (e.g., by competition).
-
The sequences of mouse RHAMM peptides and the corresponding sequences of human RHAMM are conserved in the evolution.
Key Features
-
Due to the fact that the shorter RHAMM peptide is short in size, it may have the potential to be converted into tablets for oral treatment of diabetes
-
Development of RHAMM peptides is relatively short and production cost is relatively cheap
-
Peptides, which are designed to maintain disease-specific activity, display a therapeutic activity, which seems to be not accompanied by complications and side effects
Development Milestones
Seeking funding for completing the preclinical project and for clinical studies
Additional indications
May also applicable for malignant diseases
1586128900.png)