We would like to perform a protein symmetrization but wonder if the presence of glycerol or any stabilizing protein can prevent spontaneous oligomerization in solution. Could it be an issue?
Thank you in advance for your suggestions!
Dear Hana
it is a difficult question because it depends a lot from the properties of the protein
eg. why it agggregate?
Is it a well folded but form oligomers to the presence of charged or hydrophobic patches of the surface?
Is it unfolded?
Is it a membrane protein?
and the reason why the component is able to stop the aggregation.
For example.
In my experience the addition of glycerol in several case is able to prevent the protein aggregation when protein are stored at -20°C but i think that it is due to the fact that it protect the protein from unfolding which could be determined to the volume expansion that happen when water solidify and the aggregation is a secondary effect of the unfolding.
Similarly arginine is reported to protect proteins from aggregation but is not so clear if it affect the folding or similarly to urea is just able to mantain in solution unfolded proteins.
Ciao
Manuele
Dear Manuele,
thank you for your answer! Your answer showed me a good direction of what I should look for :)
Our protein is folded well but we know there are hydrophobic side chains and suppose that its assembly is primarily mediated by electrostatic interaction. So I assume that pH is the most important.
This paper gave me a few suggestions: https://pubmed.ncbi.nlm.nih.gov/19817484/
Best
Hana
Dear Hana,
As mentioned, glycerol is used as an effective mediator to stabilize proteins in solution (especially during protein purification).
Hence, if the oligomerization is at any point driven via hydrophobic groups then that might be a case of concern.
That being said, however, I think that an optimization of the glycerol concentration can be performed.
Alternatively, other stabilizers can also be looked at.
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