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The First Water‐Soluble 3 10 ‐Helical Peptides
Author(s) -
Formaggio Fernando,
Crisma Marco,
Rossi Paola,
Scrimin Paolo,
Kaptein Bernard,
Broxterman Quirinus B.,
Kamphuis Johan,
Toniolo Claudio
Publication year - 2000
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/1521-3765(20001215)6:24<4498::aid-chem4498>3.0.co;2-4
Subject(s) - propanoic acid , amino acid , amino acid residue , chemistry , helix (gastropod) , sequence (biology) , peptide , stereochemistry , peptide sequence , ternary operation , water soluble , biochemistry , biology , organic chemistry , computer science , ecology , snail , gene , programming language
Two water‐soluble 3 10 ‐helical peptides are synthesized and fully characterized for the first time. The sequence of these terminally blocked heptamers comprises two residues of the C α ‐trisubstituted α‐amino acid 2‐amino‐3‐[1‐(1,4,7‐triazacyclononyl)]propanoic acid and five residues of a C α ‐tetrasubstituted α‐amino acid (either α‐aminoisobutyric acid or isovaline). Using CD and NMR techniques we were able to show that both heptapeptides are well structured in water, and that the type of conformation adopted is indeed the ternary 3 10 ‐helix.