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Crystal structure of a tripeptide containing aminocyclododecane carboxylic acid: a supramolecular twisted parallel β‐sheet in crystals
Author(s) -
Vasudev Prema G.,
Aravinda Subrayashastri,
Shamala Narayanaswamy
Publication year - 2016
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2854
Subject(s) - tripeptide , supramolecular chemistry , ramachandran plot , crystallography , dipeptide , chemistry , peptide , beta sheet , stereochemistry , crystal structure , supramolecular assembly , side chain , residue (chemistry) , liquid crystal , protein structure , materials science , organic chemistry , polymer , biochemistry , optoelectronics
The crystal structure of a tripeptide Boc‐Leu‐Val‐Ac 12 c‐OMe ( 1 ) is determined, which incorporates a bulky 1‐aminocyclododecane‐1‐carboxylic acid (Ac 12 c) side chain. The peptide adopts a semi‐extended backbone conformation for Leu and Val residues, while the backbone torsion angles of the C α,α ‐dialkylated residue Ac 12 c are in the helical region of the Ramachandran map. The molecular packing of 1 revealed a unique supramolecular twisted parallel β‐sheet coiling into a helical architecture in crystals, with the bulky hydrophobic Ac 12 c side chains projecting outward the helical column. This arrangement resembles the packing of peptide helices in crystal structures. Although short oligopeptides often assemble as parallel or anti‐parallel β‐sheet in crystals, twisted or helical β‐sheet formation has been observed in a few examples of dipeptide crystal structures. Peptide 1 presents the first example of a tripeptide showing twisted β‐sheet assembly in crystals. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.