Residue requirements for helical folding in short α/β-peptides: Crystallographic characterization of the 11-helix in an optimized sequence

Margaret A. Schmitt, Soo Hyuk Choi, Ilia A. Guzei, Samuel H. Gellman

Research output: Contribution to journalArticle

100 Citations (Scopus)

Abstract

Design of functional foldamers requires knowledge of the conformational propensities of constituent residues. Here, we explore the effects of variations in both α-amino acid and β-amino acid substitution on α/β-peptide helicity. We also report the first X-ray crystal structure of a helical α/β-peptide. We conclude that a certain amount of conformational preorganization in α;/β-peptides (via the inclusion of constrained β-amino acids or α,α-disubstituted α-amino acids) is needed to promote helical folding; acyclic β-amino acids and β-branched α-amino acids are tolerated to only a limited extent.

Original languageEnglish
Pages (from-to)13130-13131
Number of pages2
JournalJournal of the American Chemical Society
Volume127
Issue number38
DOIs
Publication statusPublished - 2005 Sep 28

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Peptides
Amino acids
Amino Acids
Acyclic Acids
Amino Acid Substitution
X-Rays
Substitution reactions
Crystal structure
X rays

All Science Journal Classification (ASJC) codes

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

Cite this

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title = "Residue requirements for helical folding in short α/β-peptides: Crystallographic characterization of the 11-helix in an optimized sequence",
abstract = "Design of functional foldamers requires knowledge of the conformational propensities of constituent residues. Here, we explore the effects of variations in both α-amino acid and β-amino acid substitution on α/β-peptide helicity. We also report the first X-ray crystal structure of a helical α/β-peptide. We conclude that a certain amount of conformational preorganization in α;/β-peptides (via the inclusion of constrained β-amino acids or α,α-disubstituted α-amino acids) is needed to promote helical folding; acyclic β-amino acids and β-branched α-amino acids are tolerated to only a limited extent.",
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Residue requirements for helical folding in short α/β-peptides : Crystallographic characterization of the 11-helix in an optimized sequence. / Schmitt, Margaret A.; Choi, Soo Hyuk; Guzei, Ilia A.; Gellman, Samuel H.

In: Journal of the American Chemical Society, Vol. 127, No. 38, 28.09.2005, p. 13130-13131.

Research output: Contribution to journalArticle

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T1 - Residue requirements for helical folding in short α/β-peptides

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AU - Schmitt, Margaret A.

AU - Choi, Soo Hyuk

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AU - Gellman, Samuel H.

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