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Solid‐phase synthesis and purification of a set of uniformly 13 C, 15 N labelled de novo designed membrane fusogenic peptides
Author(s) -
Agrawal Prashant R.,
Hofmann Mathias W.,
Meeuwenoord Nico J.,
Filippov Dmitri V.,
Stalz Holger,
Hulsbergen Frans,
Langosch Dieter,
Overkleeft Hermen S.,
De Groot Huub
Publication year - 2007
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.786
Subject(s) - membrane , transmembrane protein , peptide , amino acid , lipid bilayer fusion , chemistry , yield (engineering) , fusion , biophysics , biochemistry , biology , materials science , receptor , linguistics , philosophy , metallurgy
The transmembrane segments of soluble N ‐ethylmaleimide‐sensitive factor (SNARE) proteins or viral envelope proteins drive membrane fusion, which suggests that simple synthetic biology constructs for fusion exist and can be evaluated. We describe the high‐yield synthesis of a set of de novo designed fusogenic peptides for use in functional investigations, which are highly enriched in 13 C and 15 N using three equivalents of labelled amino acids and optimized reaction conditions minimizing aggregation. The biomimetic peptides have a high purity >90% and show reproducible and fusogenic activity that correlates well with the intended functional design characteristics, from strongly fusogenic to almost non‐fusogenic. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.