(Total Views: 892)
Posted On: 02/25/2022 8:19:10 AM
Post# of 148878
Here is an old post, brought up by Guy on YMB. Sometimes it is nice to be reminded of what we have:
"Here’s an old post (a couple of years ago) from Ed (a scientist) regarding Leronlimab’s HIV data.
Ed:
Actually, its probably far better than most dedicated shareholders even know. If you go back and look at the 2010 clinical trials, what you find is that 162mg biweekly of leronlimab (LL) can reduce viral load by 90% after 4 weeks, 326mg biweely will reduce it by 96% and 326mg weekly for 4 weeks will reduce it by 98%. That should tell you that LL sticks to CCR5 better than any other CCR5 blocker out there. Compare that to maraviroc which requires 300mg twice daily, and that should tell you that maraviroc only sticks for around 12 hours.
That means maraviroc is throwing 600mg per day of byproducts at the liver and kidneys, which should help everyone understand why its somewhat toxic to both organs. So what we have here is a drug that binds to CCR5 incredibly well, and if there is a medial need for that, then we have solved it better than anybody else.
If you study Dr. Maddon and his reasoning behind how he created LL, you would discover that he hunted for the very best monoclonal antibody he could create. And of course, to understand that, you need to understand how mAbs are created in the first place.
To create a mAb, they inject an immunogen into a rat or other animal to elicit an immune response. This is a brilliant use of nature to solve a problem for us. If we want an antibody that fights a virus, we can study the B-leukocytes that are creating antibodies that fight that virus. By injecting human CCR5 into the rat, we get antibodies that fight human CCR5! And that's how we created B-cells that make antibodies that bind to CCR5.
Once you have a rat making antibodies, researchers extract the B-cells from the spleen and then fuse them with human cancer cells called myelomas, to create a hybridoma. These are super-antibody factories because they have the infinite reproductive powers of cancer combined with the B-cell's antibody producing capabilities. Researchers then take each of the hybridomas, put them in their own private petri dish, and then study each one to see which one is making the best antibodies.
You see, each B-cell has its own unique way of fighting the immunogen. Each might bind (attack) the immunogen's protein strands in different locations, so its up to researchers to figure out which ones are better than the others. In the case of Dr. Maddon, he specifically sought out the mAb that binded to CCR5 in exactly the same way that HIV does. And that makes perfect sense because his goal was to stop HIV from binding to CCR5. No clue where it was just serendipity or pure genius, but this yielded one extremely effective CCR5 blocker! Maybe HIV has had thousands of years to evolve and during that evolution, myriad different permutations failed to bind until one finally found a way to attach to something in human immune cells. Dunno, don't really care. What matters here is that this drug is perhaps the most effective at binding to CCR5 of anything out there.
The next question we should have is, "how valuable is being able to block CCR5?" We already know its highly effective at treating HIV, so that's one market we could dominate. We also know that it shows incredible promise against some cancers, and that's another market we can enter and save a lot of lives. Lastly, we know that our success in modulating the immune system suggests we can do great things to help patients with autoimmune conditions: MS, Lupus, IBS, eczema, psoriasis, and many others.
I'm a scientist so I don't go around trying to explain why it hasn't been approved or acquired. Those are man-made issues that can be easily corrected. I've covered the God-made (or nature-made for those of you God-deniers) issues, as those are written in biology and physics, and not really subject to the whims of man."
"Here’s an old post (a couple of years ago) from Ed (a scientist) regarding Leronlimab’s HIV data.
Ed:
Actually, its probably far better than most dedicated shareholders even know. If you go back and look at the 2010 clinical trials, what you find is that 162mg biweekly of leronlimab (LL) can reduce viral load by 90% after 4 weeks, 326mg biweely will reduce it by 96% and 326mg weekly for 4 weeks will reduce it by 98%. That should tell you that LL sticks to CCR5 better than any other CCR5 blocker out there. Compare that to maraviroc which requires 300mg twice daily, and that should tell you that maraviroc only sticks for around 12 hours.
That means maraviroc is throwing 600mg per day of byproducts at the liver and kidneys, which should help everyone understand why its somewhat toxic to both organs. So what we have here is a drug that binds to CCR5 incredibly well, and if there is a medial need for that, then we have solved it better than anybody else.
If you study Dr. Maddon and his reasoning behind how he created LL, you would discover that he hunted for the very best monoclonal antibody he could create. And of course, to understand that, you need to understand how mAbs are created in the first place.
To create a mAb, they inject an immunogen into a rat or other animal to elicit an immune response. This is a brilliant use of nature to solve a problem for us. If we want an antibody that fights a virus, we can study the B-leukocytes that are creating antibodies that fight that virus. By injecting human CCR5 into the rat, we get antibodies that fight human CCR5! And that's how we created B-cells that make antibodies that bind to CCR5.
Once you have a rat making antibodies, researchers extract the B-cells from the spleen and then fuse them with human cancer cells called myelomas, to create a hybridoma. These are super-antibody factories because they have the infinite reproductive powers of cancer combined with the B-cell's antibody producing capabilities. Researchers then take each of the hybridomas, put them in their own private petri dish, and then study each one to see which one is making the best antibodies.
You see, each B-cell has its own unique way of fighting the immunogen. Each might bind (attack) the immunogen's protein strands in different locations, so its up to researchers to figure out which ones are better than the others. In the case of Dr. Maddon, he specifically sought out the mAb that binded to CCR5 in exactly the same way that HIV does. And that makes perfect sense because his goal was to stop HIV from binding to CCR5. No clue where it was just serendipity or pure genius, but this yielded one extremely effective CCR5 blocker! Maybe HIV has had thousands of years to evolve and during that evolution, myriad different permutations failed to bind until one finally found a way to attach to something in human immune cells. Dunno, don't really care. What matters here is that this drug is perhaps the most effective at binding to CCR5 of anything out there.
The next question we should have is, "how valuable is being able to block CCR5?" We already know its highly effective at treating HIV, so that's one market we could dominate. We also know that it shows incredible promise against some cancers, and that's another market we can enter and save a lot of lives. Lastly, we know that our success in modulating the immune system suggests we can do great things to help patients with autoimmune conditions: MS, Lupus, IBS, eczema, psoriasis, and many others.
I'm a scientist so I don't go around trying to explain why it hasn't been approved or acquired. Those are man-made issues that can be easily corrected. I've covered the God-made (or nature-made for those of you God-deniers) issues, as those are written in biology and physics, and not really subject to the whims of man."
(29)
(0)Scroll down for more posts ▼
