You might be able to moderate the aggregation by either increasing or decreasing the salt concentration.

If the protein is less prone to aggregate at pH 8, then why not keep it at pH 8?

It might help to add a non-denaturing detergent.

Hi Adam B Shapiro ! I need to decrease de pH to do some NMR acquisition. If the pH is to high the amidics hidrogens are not visible well. There´s a huge conformational change.

Add SDS help me by stabilizing the structure at low concentrations but does not work in higher concentrations.

But i´ll try change the salt concentration.

thanks!

SDS is not an appropriate detergent because it is denaturing. There are many nondenaturing detergents you could try, such as CHAPS, n-octylglucoside, dodecylmaltoside and many others.

I just have tried CHAPS, but i´ll try the others.

Thanks!

SDS at 0.2% (7mM) is safe to use. You can also try to wash it out on the Amicon filter.

Hi Petr Rathner I´m using 0.1% SDS wich works in low concentration. The amicon doen´t work to decrease pH because the protein aggregates too.

Thanks for the answer!

Hi Dr Antonio Casalinho . See the link: https://info.gbiosciences.com/blog/tips-for-preventing-protein-aggregation-loss-of-protein-solubility

See the following link: https://www.pharmtech.com/view/excipient-selection-protein-stabilization

See also the following RG link: Article Mechanisms of Protein Stabilization and Prevention of Protei...

Also see the following link: https://www.google.com/amp/s/info.gbiosciences.com/blog/tips-for-preventing-protein-aggregation-loss-of-protein-solubility%3Fhs_amp%3Dtrue

Kindly see also the following link: https://www.biozentrum.unibas.ch/fileadmin/redaktion/05_Facilities/01_Technology_Platforms/BF/Protocols/Preventing_Protein_Aggregation.pdf

Aref Wazwaz thank you!

You are most welcome dear Antonio Casalinho .

Wish you the best always.