TEMPLATE ASSEMBLED SYNTHETIC PROTEINS - CONDENSATION OF A MULTIFUNCTIONAL PEPTIDE TO A TOPOLOGICAL TEMPLATE VIA CHEMOSELECTIVE LIGATION

Authors
Citation
G. Tuchscherer, TEMPLATE ASSEMBLED SYNTHETIC PROTEINS - CONDENSATION OF A MULTIFUNCTIONAL PEPTIDE TO A TOPOLOGICAL TEMPLATE VIA CHEMOSELECTIVE LIGATION, Tetrahedron letters, 34(52), 1993, pp. 8419-8422
Citations number
20
Categorie Soggetti
Chemistry Inorganic & Nuclear
Journal title
ISSN journal
00404039
Volume
34
Issue
52
Year of publication
1993
Pages
8419 - 8422
Database
ISI
SICI code
0040-4039(1993)34:52<8419:TASP-C>2.0.ZU;2-I
Abstract
A chemoselective ligation via oxime bond formation is used for the che mical synthesis of template assembled peptides according to the TASP ( Template Assembled Synthetic Proteins) approach. Aminooxyacetylation o f the multifunctional partial sequence Lys- Arg- Asp- Ser of lactoferr in and subsequent condensation in aqueous solution with a topological template containing four selectively addressable aldehyde functions as attachment sites gives readily access to the TASP molecule.