Computational investigation of retro-isomer equilibrium structures: Intrinsically disordered, foldable, and cyclic peptides

Gül H. Zerze, Frank H. Stillinger, Pablo Gaston Debenedetti

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

We use all-atom modeling and advanced-sampling molecular dynamics simulations to investigate quantitatively the effect of peptide bond directionality on the equilibrium structures of four linear (two foldable, two disordered) and two cyclic peptides. We find that the retro forms of cyclic and foldable linear peptides adopt distinctively different conformations compared to their parents. While the retro form of a linear intrinsically disordered peptide with transient secondary structure fails to reproduce a secondary structure content similar to that of its parent, the retro form of a shorter disordered linear peptide shows only minor differences compared to its parent.

Original languageEnglish (US)
Pages (from-to)104-113
Number of pages10
JournalFEBS Letters
Volume594
Issue number1
DOIs
StatePublished - Jan 1 2020

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Keywords

  • cyclic peptides
  • intrinsically disordered peptides
  • p53
  • peptidomimetics
  • retro peptides

Fingerprint Dive into the research topics of 'Computational investigation of retro-isomer equilibrium structures: Intrinsically disordered, foldable, and cyclic peptides'. Together they form a unique fingerprint.

  • Cite this