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Preparation of truncated orf virus entry fusion complex proteins by chemical synthesis
Author(s) -
Yeung Ho,
Harris Paul W. R.,
Squire Christopher J.,
Baker Edward N.,
Brimble Margaret A.
Publication year - 2014
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2627
Subject(s) - native chemical ligation , subfamily , peptide , fusion protein , chemistry , lipid bilayer fusion , chemical synthesis , computational biology , solid phase synthesis , biochemistry , combinatorial chemistry , biology , membrane , recombinant dna , in vitro , gene
Members of the Chordopoxvirinae subfamily possess an unusual 11 protein entry–fusion complex (EFC) that is highly conserved and present in all species. The mode of action of this EFC is unknown, and the interactions of the constituent proteins are uncharacterised. Here, we present the chemical synthesis of membrane domain truncated linear constructs of two EFC proteins in orf virus, ORFV036 and 049. By using Boc solid phase peptide synthesis and native chemical ligation methods, these truncated proteins have been readily prepared in milligram quantities. These robust synthetic protocols allow ready access to these polypeptides to facilitate biological studies. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.