CO....leading light12 Jan 2022 11:23
from another thread the cautious optimist wrote
**"Likewise, perhaps having the Affimer relatively “unencumbered” and mobile in the sample fluid gives it maximum chance to locate and latch onto the spikes."**
search, grab, and immobilise on T-line job of the affimer, and sentence above is a clear benefit of an affimer. No one else said it but helped me out of my funk. Good point CO.
Having a molecule that can show colour and can grab same protein isn't so tough, it doesn't need to be specific. If the antibody GRABS a protein from some other virus, so what, it will flow past T-line and show up at C. This problem is caused by the antibody being pretty specific, but too sensitive to mutations.
Avacta should be using this as proof that affimers are better than antibody test. Being smaller, and a lot more targeted, mutation doesn't affect them so much. The affirmer doesn't care what the rest of protein looks like, it can change all it likes, the affimer still hits the binding site. The antibody is so affected by changes all over the protein which are a lot more. Of course if affimer binding site changes/blocked the affimer is buggered, but given that the site is essential for infection maybe thats a lot lower risk.
So a paper about why did this LGD fail ie a why antibodies LFDs are not good at coping with mutation would actually improve Avacata position. Go on the attack, show why affimers are better.
Shame the antibody chosen was so targeted, maybe a less specific antibody combined with highly specific affirmer is perfect mix. Maybe why Deepverge mix with aptemers.
End of day it's an expensive lesson. Also my knowledge on this level of molecular engineering is old and rudimentary, so might be way off base.
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