My work requires gel electrophoresis of some truncated peptides aggregates (less then 10 residues long containing aromatic aa in between) in their native form. I cannot opt for using SDS because it destroys the native state of the peptide. Considering the fact that truncated variants do not obey the law of mass/mobility relationship that most protein follow in conventional SDS/Native PAGE, can anyone suggest me a way to separate out different sizes (dimer, trimer etc) of my peptide aggregates.
Did you say that your peptides are less than 10 amino acids long? If so you can just synthesize them one by one, and in that case of course no separations are needed.
Dear Vicente,
yes my peptides are 10amino acids long. I want to separate the peptide aggregates rather than different peptides from a solution.
Jahnu
You may try HPLC to separate aggregates from soluble peptides, I suggest to check aggregates size by laser light scatering. Alternatively, solid phase separation by Sepack columns might be helpful.
- Badges
- Science method