Crystallographic characterization of helical secondary structures in α/β-peptides with 1:1 residue alternation

Hyuk Choi Soo, Ilia A. Guzei, Lara C. Spencer, Samuel H. Gellman

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

Oligomers that contain both α- and β-amino acid residues in a 1:1 alternating pattern have recently been shown by several groups to adopt helical secondary structures in solution. The β-residue substitution pattern has a profound effect on the type of helix formed and the stability of the helical conformation. On the basis of two-dimensional NMR data, we have previously proposed that β-residues with a five-membered ring constraint promote two different types of α/β-peptide helix. The "11-helix" contains i,i+3 C=O⋯H-N hydrogen bonds between backbone amide groups; these hydrogen bonds occur in 11-atom rings. The α/β-peptide "14/15-helix" contains i,i+A C=O⋯H-N hydrogen bonds, which occur in alternating 14- and 15-atom rings. Here we provide crystallographic data for 14 α/β-peptides that form the 11-helix and/or the 14/15-helix. These results were obtained for a series of oligomers containing β-residues derived from (S,S)-trans-2- aminocyclopentanecarboxylic acid (ACPC) and α-residues derived from α-aminoisobutyric acid (Aib) or L-alanine (Ala). The crystallized α/β-peptides range in length from 4 to 10 residues. Nine of the α/β- peptides display the 11-helix in the solid state, three display the 14/15-helix, and two display conformations that contain both i,i+3 and i,i+4 C=O⋯H-N hydrogen bonds, but not bifurcated hydrogen bonds. Only 3 of the 14 crystal structures presented here have been previously described. These results suggest that longer α/β-peptides prefer the 14/15-helix over the 11-helix, a conclusion that is consistent with previously reported NMR data obtained in solution.

Original languageEnglish
Pages (from-to)6544-6550
Number of pages7
JournalJournal of the American Chemical Society
Volume130
Issue number20
DOIs
Publication statusPublished - 2008 May 21

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Peptides
Hydrogen
Hydrogen bonds
Oligomers
Conformations
Cycloleucine
Nuclear magnetic resonance
Aminoisobutyric Acids
Atoms
Acids
Amides
Alanine
Amino acids
Substitution reactions
Crystal structure
Display devices
Amino Acids
hydroxide ion

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

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title = "Crystallographic characterization of helical secondary structures in α/β-peptides with 1:1 residue alternation",
abstract = "Oligomers that contain both α- and β-amino acid residues in a 1:1 alternating pattern have recently been shown by several groups to adopt helical secondary structures in solution. The β-residue substitution pattern has a profound effect on the type of helix formed and the stability of the helical conformation. On the basis of two-dimensional NMR data, we have previously proposed that β-residues with a five-membered ring constraint promote two different types of α/β-peptide helix. The {"}11-helix{"} contains i,i+3 C=O⋯H-N hydrogen bonds between backbone amide groups; these hydrogen bonds occur in 11-atom rings. The α/β-peptide {"}14/15-helix{"} contains i,i+A C=O⋯H-N hydrogen bonds, which occur in alternating 14- and 15-atom rings. Here we provide crystallographic data for 14 α/β-peptides that form the 11-helix and/or the 14/15-helix. These results were obtained for a series of oligomers containing β-residues derived from (S,S)-trans-2- aminocyclopentanecarboxylic acid (ACPC) and α-residues derived from α-aminoisobutyric acid (Aib) or L-alanine (Ala). The crystallized α/β-peptides range in length from 4 to 10 residues. Nine of the α/β- peptides display the 11-helix in the solid state, three display the 14/15-helix, and two display conformations that contain both i,i+3 and i,i+4 C=O⋯H-N hydrogen bonds, but not bifurcated hydrogen bonds. Only 3 of the 14 crystal structures presented here have been previously described. These results suggest that longer α/β-peptides prefer the 14/15-helix over the 11-helix, a conclusion that is consistent with previously reported NMR data obtained in solution.",
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Crystallographic characterization of helical secondary structures in α/β-peptides with 1:1 residue alternation. / Soo, Hyuk Choi; Guzei, Ilia A.; Spencer, Lara C.; Gellman, Samuel H.

In: Journal of the American Chemical Society, Vol. 130, No. 20, 21.05.2008, p. 6544-6550.

Research output: Contribution to journalArticle

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T1 - Crystallographic characterization of helical secondary structures in α/β-peptides with 1:1 residue alternation

AU - Soo, Hyuk Choi

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N2 - Oligomers that contain both α- and β-amino acid residues in a 1:1 alternating pattern have recently been shown by several groups to adopt helical secondary structures in solution. The β-residue substitution pattern has a profound effect on the type of helix formed and the stability of the helical conformation. On the basis of two-dimensional NMR data, we have previously proposed that β-residues with a five-membered ring constraint promote two different types of α/β-peptide helix. The "11-helix" contains i,i+3 C=O⋯H-N hydrogen bonds between backbone amide groups; these hydrogen bonds occur in 11-atom rings. The α/β-peptide "14/15-helix" contains i,i+A C=O⋯H-N hydrogen bonds, which occur in alternating 14- and 15-atom rings. Here we provide crystallographic data for 14 α/β-peptides that form the 11-helix and/or the 14/15-helix. These results were obtained for a series of oligomers containing β-residues derived from (S,S)-trans-2- aminocyclopentanecarboxylic acid (ACPC) and α-residues derived from α-aminoisobutyric acid (Aib) or L-alanine (Ala). The crystallized α/β-peptides range in length from 4 to 10 residues. Nine of the α/β- peptides display the 11-helix in the solid state, three display the 14/15-helix, and two display conformations that contain both i,i+3 and i,i+4 C=O⋯H-N hydrogen bonds, but not bifurcated hydrogen bonds. Only 3 of the 14 crystal structures presented here have been previously described. These results suggest that longer α/β-peptides prefer the 14/15-helix over the 11-helix, a conclusion that is consistent with previously reported NMR data obtained in solution.

AB - Oligomers that contain both α- and β-amino acid residues in a 1:1 alternating pattern have recently been shown by several groups to adopt helical secondary structures in solution. The β-residue substitution pattern has a profound effect on the type of helix formed and the stability of the helical conformation. On the basis of two-dimensional NMR data, we have previously proposed that β-residues with a five-membered ring constraint promote two different types of α/β-peptide helix. The "11-helix" contains i,i+3 C=O⋯H-N hydrogen bonds between backbone amide groups; these hydrogen bonds occur in 11-atom rings. The α/β-peptide "14/15-helix" contains i,i+A C=O⋯H-N hydrogen bonds, which occur in alternating 14- and 15-atom rings. Here we provide crystallographic data for 14 α/β-peptides that form the 11-helix and/or the 14/15-helix. These results were obtained for a series of oligomers containing β-residues derived from (S,S)-trans-2- aminocyclopentanecarboxylic acid (ACPC) and α-residues derived from α-aminoisobutyric acid (Aib) or L-alanine (Ala). The crystallized α/β-peptides range in length from 4 to 10 residues. Nine of the α/β- peptides display the 11-helix in the solid state, three display the 14/15-helix, and two display conformations that contain both i,i+3 and i,i+4 C=O⋯H-N hydrogen bonds, but not bifurcated hydrogen bonds. Only 3 of the 14 crystal structures presented here have been previously described. These results suggest that longer α/β-peptides prefer the 14/15-helix over the 11-helix, a conclusion that is consistent with previously reported NMR data obtained in solution.

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