biOasis Technologies Ord Shs V.BTI.H

RE:RE:RE:RE:RE:RE:RE:RE:RE:Transcendpep vs. Angiopep

[BearDownAZ]

Angiopep's lead compound ANG1005 is not a fusion protein, but a conjugate. However, the compound that the Angiopep-2 peptide is attached to is not a protein, it is a small molecule called Paclitaxel (https://en.wikipedia.org/wiki/Paclitaxel). One cannot make a fusion protein between a peptide and a small molecule such as this one. It was pointed out that Angiopep has done some pre-clinical work with fusion proteins as well. So in this regards, is seems that Angiochem and Bioasis are on equal footing..both having targeting peptides that can be used to conjugate to compound of choice or to make fusion proteins. But as JD pointed out, it seems that Bioasis is going 100% forward with fusion proteins for applications amenable to fusion proteins. Perhaps Angiochem is doing the same?

For enzyme replacement, such as the LSD program, yes fusion proteins are the way to go. By cloning in the DNA sequence encoding the targeting peptide into the DNA sequence corresponding to the enzyme, the resulting mRNA encoded by this DNA contains sequences for both the enzyme and the peptide "fused" together and the resulting protein translated from this mRNA features the targeting peptide in the same location of the enzyme every time. Fusion protein implies that there are two amino acid/protein components that are linked together during the tranlation of the mRNA to protein.   

Same thing applies to antibody therapies. Antibodies are proteins.....so fusion proteins are the way to go. Instead of conjugating together antibodies and targeting peptides that were each synthesized separately, make a fusion protein. 

However, for small molecules (such as Paclitaxel above) you cannot make a fusion protein since the drug is not a protein. This is a limitation for both Bioasis and Angiochem. I believe conjugation is their only option here. However, there may be some additional steps in the conjugation process that can help make the conjugation site between the peptide and the drug more reproducible.

What about siRNAs? siRNAs are also not proteins.....no amino acids. So they can't be fusion proteins. I imagine they are conjugating the targeting peptide to the siRNA, and therefore the siRNA and peptide are produced separately from one another. But perhaps they have a few tricks up their sleeve in the biosynthesis of the siRNA and peptide that allows for a reproducible site of conjugation.

Just a few morning thoughts. Have a great day everyone.