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Updated: Mar 23, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Ribbon structure stabilized by C10 and C12 turns in αγ hybrid peptide
Naiem Ahmad Wani1, Rajni Kant2, Vivek Kumar Gupta2
1Medicinal Chemistry Division, Indian Institute of Integrative Medicine, Canal Road, Jammu Tawi, 180001, India.
Abstract:
The present study describes the synthesis and crystallographic analysis of αγ hybrid peptides, Boc-Gpn-L-Pro-NHMe (1), Boc-Aib-Gpn-L-Pro-NHMe (2), and Boc-L-Pro-Aib-Gpn-L-Pro-NHMe (3). Peptides 1 and 2 adopt expanded 12-membered (C12 ) helical turn over γα segment. Peptide 3 promotes the ribbon structure stabilized by type II β-turn (C10 ) followed by the expanded C12 helical γα turn. Both right-handed and left-handed helical conformations for Aib residue are observed in peptides 2 and 3, respectively.
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