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Synthesis of a template‐associated peptide designed as a transmembrane ion channel former
Author(s) -
Chaloin Laurent,
Méry Jean,
Van Mau Nicole,
Divita Gilles,
Heitz Frédéric
Publication year - 1999
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/(sici)1099-1387(199909)5:9<381::aid-psc206>3.0.co;2-l
Subject(s) - transmembrane protein , ion channel , peptide , chemistry , combinatorial chemistry , nanotechnology , biophysics , biochemistry , materials science , biology , receptor
We describe the design and the Fmoc/ t Bu solid phase synthesis of a 20 residue long peptide containing five regularly distributed lysines. Cyclization of this peptide was achieved using BOP as coupling agent. After side‐chain deprotection, all the basic residues were iodoacetylated and then allowed to react either with a C ‐terminal free COOH peptide or with peptides bearing a cysteamide group. The final pentameric templates were identified by mass and amino acid analysis which gave data compatible with the expected values. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd.