At 08:48 AM 9/21/00 -0700, Gordon Alton wrote:
> Dear ABRFers, I am trying to form a disulfide bond between two fully
>deprotected peptides. One is a very basic 10mer with a C-terminal cysteine
>and the other is a neutral 4mer with a N-terminal cysteine. Does anyone
>have any suggestions (conditions) on how to promote the disulfide
>formation or references concerning this? In advance, thanks.
>--------------------------------------------------------
>Gordon Alton, Ph.D. Analytical/Protein Chemistry and Mass Spectrometry
>Signal Pharmaceuticals Inc.
>5555 Oberlin Drive
>San Diego, CA 92121 galton@signalpharm.com
> 858-558-7500 x8252
> 858-623-0870
> http://www.signalpharm.com
>-------------------------------------------------
Gordon,
I have had great success using DTNB (Ellman's rgt) for this purpose.
React one of the peptides with this rgt and let the other one with the free
SH displace the TNB group via a thiol-disulfide exchange rxn. Works very
well and all products are easy to follow by RP-HPLC or SCX-HPLC. See
Peptide Research (1989) 2, 395-401 for detailed reaction info.
Good luck,
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