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Updated: Jun 24, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Noncanonical Folding of Peptoid Oligomers: Formation of a Closed Conformation in Nonpolar Solvent
Jinyoung Oh1, Min June Yang1, Xingyu Chen2
1Department of Chemistry, Gwangju Institute of Science and Technology, 123 Cheomdangwagi-ro, Buk-gu, Gwangju 61005, Republic of Korea.
Abstract:
Conformational behavior of peptoids in low-dielectric solvents remains poorly understood despite its relevance to membrane environments. Here, conformations of N-(S)-1-phenylethylglycine (Nspe) homo-oligomers were investigated in chloroform using NMR spectroscopy and MD simulations. Nspe7 populated two closed conformations, while Nspe10 adopted a single conformation reminiscent of the Nspe9 threaded-loop structure. End-to-end hydrogen bonding and hydrophobic side-chain shielding stabilize these compact folds, minimizing polar surface area. These findings provide insights into peptoid folding in nonpolar media and solvent-directed conformational switching.
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