Jose Brandao-Neto
answered on 14 Nov 2019:
last edited 14 Nov 2019 1:06 pm
Hi!
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crystals can make xrays change direction and that can be exploited to understand what was inside the crystal, like, actual positions of the atoms inside the crystal.
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So, if you convince proteins-important-in-a-disease-condition to form crystals you can **shoot protein crystals with xrays** to understand the protein shape inside the crystal. If you know that, you can literally rinse the crystals with a solution of a would-be medicine (not joking) and then you can ‘see’ how the medicine binds to the protein.
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Because, in 2019, what you usually want is to prevent certain protein types from doing what they normally do and that way stop the disease (or kill weeds or kill bacteria). And if you know the interaction protein:would-be-medicine, your chemist friend can create would-be-medicines which stick better to protein types – so proteins stop doing what they normally do. Mind you, there are some 10,000 different protein types in each type of organism (human, plant, bacteria etc) .
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For the last 70 years this process of getting from would-bes to medicines takes about 20 years.
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Cheers,
Jose’
check this paper, my collaborator in this work can rank would-be drugs with an electrophysiology experiment. they work on a drug to prevent people from relapsing into smoking, similar to those patches.
In this case, the target protein did not want to become a crystal, so they used a snail protein, modified it to behave like a human protein and then crystallised it.
start with the abstract and then jump to the conclusion (pun not intended): http://www.jbc.org/content/293/7/2534
An allosteric binding site of the α7 nicotinic acetylcholine receptor revealed in a humanized acetylcholine-binding protein
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Jose commented on :
check this paper, my collaborator in this work can rank would-be drugs with an electrophysiology experiment. they work on a drug to prevent people from relapsing into smoking, similar to those patches.
In this case, the target protein did not want to become a crystal, so they used a snail protein, modified it to behave like a human protein and then crystallised it.
start with the abstract and then jump to the conclusion (pun not intended):
http://www.jbc.org/content/293/7/2534
An allosteric binding site of the α7 nicotinic acetylcholine receptor revealed in a humanized acetylcholine-binding protein