Hi,
That depends, I guess.
Did you synthesize peptides and would you like to purify the final products from impurities? Or something else?
What amounts would you like to purify?
How do your peptides of interest differ most (physically) from one another; hydrophobicity, charge?
You could be looking at a (semi-)preparative reversed phase column, such as a C8 of C18 column, but in some cases, ion exchange (either cation or anion exchange) could be the better option.
The previous questions are good ones. Also, do you want to purify the peptides from everything else, or separate them from each other, or both.
There's some information floating around that suggests 200 Angstrom pores work better for this size peptide. The peptides don't fit in the smaller pores, so the additional surface area from these pores isn't available for adsorption. 200 A pores seems to be the "sweet spot" for maximizing the usable surface area for these peptides.
Depending on the characteristics of sample and impurities . C18,ion exchange,hydrophobic interaction chromatography would be ok
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