Dear John,
Nico J.C.M. Beekman et al., J. Peptide Res., 50, 1997, 357-364, proposed to use
reduction with phosphines for deprotection of Cys(StBu) in resin bound
peptides. A double deprotection of 60 min, each with 50 fold molar excess,
using tri(n-butyl)phosphine in NMP/water (9:1) under nitrogen atmosphere
suppose to completely remove the t-Buthio group.
In my practice I used double deprotection of 3 h, 30 fold molar excess of
DTT/DMF at room temperature.
Sincerely,
Boris Pekelis.
John Wade wrote:
> Dear All,
>
> Does anyone have experience with, or know of, an efficient means of
> removing the thiobutyl group from cysteine while the synthetic peptide
> remains on the solid support? The only reference I have is Eritja et al
> (Tetrahedron, 43, 2675, 1987) who used mercaptoethanol:DMF (1:1, v/v) for 5
> hours at r.t. Is there a more rapid means?
>
> Thanks in advance for any advice.
>
> John Wade
> Howard Florey Institute
> Melbourne
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