SYNTHESIS OF A DESIGNED TRANSMEMBRANE PROTEIN BY THIOETHER LIGATION OF SOLUBILIZED SEGMENTS - N-ALPHA-HALOACETYLATED PEPTIDES SURVIVED RESIN CLEAVAGE USING TFA WITH EDT AS SCAVENGER

Authors
ENGLEBRETSEN DR CHOMA CT ROBILLARD GT
Citation
Dr. Englebretsen et al., SYNTHESIS OF A DESIGNED TRANSMEMBRANE PROTEIN BY THIOETHER LIGATION OF SOLUBILIZED SEGMENTS - N-ALPHA-HALOACETYLATED PEPTIDES SURVIVED RESIN CLEAVAGE USING TFA WITH EDT AS SCAVENGER, Tetrahedron letters, 39(27), 1998, pp. 4929-4932
Citations number
15
Categorie Soggetti
Chemistry Inorganic & Nuclear
Journal title
Tetrahedron letters → ACNP
ISSN journal
00404039
Volume
39
Issue
27
Year of publication
1998
Pages
4929 - 4932
Database
ISI
SICI code
0040-4039(1998)39:27<4929:SOADTP>2.0.ZU;2-8
Abstract
N alpha-haloacetylated peptides made by Fmoc solid phase synthesis sur vived cleavage when EDT was used as a cleavage component. Two segments of a designed transmembrane protein, one bromoacetylated, the other c ontaining a cysteine, and each bearing a ''solubilising tail'' peptide , were synthesised by Fmoc SPPS. The two peptides were joined via thio ether ligation. (C) 1998 Elsevier Science Ltd. All rights reserved.