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

FEBS Letters

article

Gül H. Zerze¹  Frank H. Stillinger²  Pablo G. Debenedetti¹ 

[1] Department of Chemical and Biological Engineering, Princeton University;Department of Chemistry, Princeton University

关键词: Ab;    cyclic peptides;    intrinsically disordered peptides;    p53;    peptidomimetics;    retro peptides;   

DOI  :  10.1002/1873-3468.13558

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown