Evidence that the β-peptide 14-helix is stabilized by β3-residues with side-chain branching adjacent to the β-carbon atom

Tami L. Raguse, Jonathan R. Lai, Samuel H. Gellman

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

Oligomers of β-substituted β-amino acids ('β3-peptides') are known to adopt a helical secondary structure defined by 14-membered ring hydrogen bonds ('14-helix'). Here, we describe a deca-β3-peptide, 1, that does not adopt the 14-helical conformation and that may prefer an alternative secondary structure, β3-Peptide 1 is composed exclusively of residues with side chains that are not branched adjacent to the β-C-atom β3-hLeu, β3-hLys, and β3-hTyr). In contrast, an analogous β3-peptide, 2, containing β3-hVal residues in place of the β3-hLeu residues of 1, adopts a 14-helical conformation in MeOH, according to CD data. These results illustrate the importance of side-chain branching in determining the conformational preferences of β3-peptides.

Original languageEnglish (US)
Pages (from-to)4154-4164
Number of pages11
JournalHelvetica Chimica Acta
Volume85
Issue number12
DOIs
StatePublished - 2002
Externally publishedYes

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helices
Peptides
peptides
Carbon
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carbon
atoms
Conformations
oligomers
Oligomers
amino acids
Amino acids
Hydrogen
Hydrogen bonds
hydrogen bonds
Amino Acids
rings

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Evidence that the β-peptide 14-helix is stabilized by β3-residues with side-chain branching adjacent to the β-carbon atom. / Raguse, Tami L.; Lai, Jonathan R.; Gellman, Samuel H.

In: Helvetica Chimica Acta, Vol. 85, No. 12, 2002, p. 4154-4164.

Research output: Contribution to journalArticle

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