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Updated: Jan 21, 2026

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
Published on: September 28, 2022
Computational investigation of retro-isomer equilibrium structures: Intrinsically disordered, foldable, and cyclic
Gül H Zerze1, Frank H Stillinger2, Pablo G Debenedetti1
1Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ, USA.
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.
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