Your peptide is,definitely,more hydrophobic than anything I ever worked
with,but you can try one or all of the following.
1.You to make sure than your peptide is soluble,and it stays that way.
2.Separation can be done on a reversed phase column,starting at high
acetonitrile concentrations,even at 50%,just to see if you get anything.
I have,frequently,dissolved peptides in neat formic acid,or
acetonitrile/water with formic acid added.I was surprised to see that the
peptides disssolved,and stayed dissolved,when there was no formic acid
around.Of course,you cannot be too greedy ,trying to dissolve too much
peptide.
Fulvio Perini
UNMC
986805 Nebraska Med.Cntr.
Omaha,NE 68198-6805
gillespiep
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I have a peptide that is very hydrophobic that through trial after trial I
was
finally successful in synthesizing but now have the tough task of
purifying.
It was suggested that I check with the discussion group peptide
professionals
and see what suggestions you have on purification. I am checking to see
anyone's experience with a CN or C8 column or using pyridine/propanol on
RP-HPLC. During previous purifications the peptide was lost on the C18
column. If anyone suggests using the above procedures or has one that has
worked better for them then any information is very appreciated. Thanks in
advance.
SEQUENCE: TLVGIIVGVLLAIGF also made with C at N terminus.
Paula Gillespie
Research Assistant
University of Texas Health Science Center
San Antonio, TX 78240
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