Hi Gordon,
I had success with a similar project using 30% DMSO in 0.1% TFA. I
incubated the purified peptides together at roughly equal concentrations
and then sampled them with HPLC to monitor peak shifts. You end up with 3
products; long-long, short-short and mixed. Purify the sample with HPLC,
collect the three peaks and determine your product of interest by mass spec.
Hope this helps,
Trudy Holyst
Blood Research Institute
Peptide Core Laboratory
Blood Center of SE WI
Milwaukee WI 53201
-----Original Message-----
From: Gordon Alton [mailto:GAlton@signalpharm.com]
Sent: Thursday, September 21, 2000 10:49 AM
To: Recipients of ABRF List
Subject: disulfide bond formation
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
Email: galton@signalpharm.com
Phone: 858-558-7500 x8252
Fax: 858-623-0870
WWW: http://www.signalpharm.com <http://www.signalpharm.com/>
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