Self-association of water-soluble peptoids comprising (S)-N-1-(naphthylethyl)glycine residues

Org Lett. 2013 Oct 4;15(19):5118-21. doi: 10.1021/ol4025502. Epub 2013 Sep 19.

Abstract

Peptoids (N-substituted glycine oligomers) are widely used peptidomimetics, and an enhanced understanding of their structures is needed to expand their utility, particularly in aqueous applications. We report the synthesis and structural study of four water-soluble peptoids that include strongly helix-promoting (S)-N-1-(naphthylethyl)glycine residues. Peptoid structure changes with both peptoid length and solvent composition. Multiple data support the self-association of the longest peptoid studied here, 1, via hydrophobic interactions in aqueous solutions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Circular Dichroism
  • Crystallography, X-Ray
  • Glycine / analogs & derivatives*
  • Glycine / chemical synthesis
  • Glycine / chemistry*
  • Glycine / metabolism
  • Hydrophobic and Hydrophilic Interactions
  • N-substituted Glycines / chemistry*
  • Naphthalenes / chemical synthesis
  • Naphthalenes / chemistry*
  • Naphthalenes / metabolism
  • Peptoids / chemical synthesis*
  • Peptoids / chemistry
  • Peptoids / metabolism
  • Protein Structure, Secondary
  • Solvents / chemistry*
  • Stereoisomerism
  • Water / chemistry*

Substances

  • (S)-N-1-(naphthylethyl)glycine
  • N-substituted Glycines
  • Naphthalenes
  • Peptoids
  • Solvents
  • Water
  • Glycine