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Preferred solution conformation of peptides rich in the lipophilic, chiral, C α ‐methylated α‐amino acid (αMe)Aoc
Author(s) -
Peggion Cristina,
Formaggio Fernando,
Crisma Marco,
Toniolo Claudio,
Kaptein Bernard,
Broxterman Quirinus B.,
Kamphuis Johan
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(199912)5:12<547::aid-psc221>3.0.co;2-8
Subject(s) - random hexamer , chemistry , circular dichroism , chirality (physics) , dimer , amino acid , stereochemistry , peptide , helix (gastropod) , crystallography , organic chemistry , biochemistry , chiral symmetry , ecology , physics , quantum mechanics , snail , nambu–jona lasinio model , biology , quark
The lipophilic, chiral, C α ‐methylated α‐amino acid L ‐(αMe)Aoc (2‐methyl‐2‐amino‐octanoic acid) was prepared using a chemo‐enzymatic approach. Two series of terminally protected model peptides, from dimer through to hexamer, containing L ‐(αMe)Aoc in combination with either Gly or Aib, were synthesized by solution methods and were fully characterized. A solution conformational analysis, based on FT‐IR absorption, L H‐NMR and circular dichroism (CD) techniques, was performed with the aim at determining the preferred conformation of this novel amino acid and the relationship between chirality at its α‐carbon atom and screw sense of the helix that is formed. The results obtained strongly support the view that L ‐(αMe)Aoc favours the formation of the right ‐handed 3 10 ‐helical conformation. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd.