Dear All,
I have a small molecule containing a thiol group. I am assuming it can form a disulfide bond with a free Cysteine on my target protein. At present, I directly add the small molecule and incubate with the protein, but the small molecule cannot be bind to the target protein. Do you know any way to promote this reaction?
Thanks,
Pengcheng
A better strategy would be to modify the small molecule so that instead of having a sulfhydryl group, it has a maleimide group. This will react specifically with the surface-exposed cysteine on the protein. If you include some TCEP in the reaction, it will keep the cysteine in the reduced state for the reaction. TCEP will not react with the maleimide.
I am sorry if this is not the answer you are looking for. In technical terms, I would say any way to make a bond between two aminoacids, especially in chains with more connections, it would be the addition of a group, cysteine S-S to make a cistine, and the consequence of loosing a molecule of water. In this sense, all aminoacids loose water and make bonds like this. In fact it is the same bond we need to break to degrade an aminoacid. It would be the first treatment. (Edman degradation, but maybe the formation with adsorbtion solids. Merrifield, for example, can make aminoacids.)
Of course you need to have the right conditions. Merrifield was the first method to arrise, however, you would need to make sure other conditions are present, temperature, pH, ionic strength...). It does not require much energy.
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