Synthesis of a template-associated peptide designed as a transmembrane ion channel former.
We describe the design and the Fmoc/tBu 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.
Chaloin
L
L
CRBM, CNRS-UPR 1086, Montpellier, France.
Méry
J
J
Van Mau
N
N
Divita
G
G
Heitz
F
F
D000107:Acetylation; D000595:Amino Acid Sequence; D007473:Ion Channels / Q000138:chemical synthesis* / Q000737:chemistry; D008239:Lysine / Q000737:chemistry; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D010456:Peptides, Cyclic / Q000138:chemical synthesis; D011487:Protein Conformation; D013440:Sulfides / Q000737:chemistry; D013698:Templates, Genetic
D007473:Ion Channels; D009842:Oligopeptides; D010456:Peptides, Cyclic; D013440:Sulfides; D008239:Lysine