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First homo-peptides undergoing a reversible 3(10)-helix/alpha-helix transition: critical main-chain length.

Authors
  • Moretto, Alessandro
  • Formaggio, Fernando
  • Kaptein, Bernard
  • Broxterman, Quirinus B
  • Wu, Ling
  • Keiderling, Timothy A
  • Toniolo, Claudio
Type
Published Article
Journal
Biopolymers
Publication Date
Jan 01, 2008
Volume
90
Issue
4
Pages
567–574
Identifiers
DOI: 10.1002/bip.21016
PMID: 18481806
Source
Medline
License
Unknown

Abstract

The difference in length between the more elongated peptide 3(10)-helix and the more compact alpha-helix is about 0.4 A/residue. This property makes the 3(10)-/alpha-helix reversible conversion very promising as a molecular switching tool between the N- and C-terminal functions of a peptide backbone. In this work, using homo-peptides of various main-chain length, all based on the strongly helicogenic, Calpha-tetrasubstituted alpha-amino acid Calpha-methyl-L-valine, we show that a well defined, solvent controlled, reversible 3(10)-/alpha-helix transition takes place even in a homo-oligomer as short as a terminally blocked hexapeptide. Homo-peptide sequences blocked as a urethane or an acetamide at the N-terminus and as a methyl ester or an N-alkyl amide at the C-terminus are all appropriate. The nature of the occurring helical species in the various solvents tested was assessed by electronic or vibrational circular dichroism.

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