I have to follow the interaction between an acid and an amide.
We would like to check if they form complexes and if it is so, in which ratio. So we are interested to find a complete thermodynamic profile of the molecular interaction by measuring heat transfer during binding. As I have considered the pH should be constant during the titration. changing the pH or the temperature in the experiment may cause a decrease in the binding affinity to measurable levels.
So in my case that pH is changing. Is there any possibility to correct that pH effect?
I am not sure if it can help.I am worried if we add something which react with one of the components they interfere with the main interaction which is the reaction of amide and acid!
If I understand your problem right,the pH of the system changes along the titration, right? In this case the thermogram is a mixture of, at least, binding and pH changes. It means that the binding affinity you get is "a fake Kd" because its changing across the titration, take this into account.
You checked the pH is the same at the beginning and end of the titration? Could you provide more info about the system? Cheers!
Dear Diego
That is completely true! The pH of the system is changing during the titration. I am trying to do an acid titration and so the pH is changing continuously. Remember that I am following the interaction between the acid and an amide. Since the amide is not showing any basicity, the reaction is not very exothermic.
Hi,
I am wondering whether you use a buffer system where you run the process. Perhaps find another buffer system which is buffering in the range you see the pH change.
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