NDLI: Participation of non-aminoisobutyric acid (Aib) residues in the 3<sub>10</sub> helical conformation of Aib-rich foldamers: a solid state study

Content Provider	Royal Society of Chemistry (RSC)
Author	Pike, Sarah J. Clayden, Jonathan Raftery, James Webb, Simon J. Boddaert, Thomas
Copyright Year	2015
Abstract	The solid state conformational preferences of a series of 2-aminoisobutyric acid (Aib) foldamers bearing a single N-terminal tertiary amino acid (Cbz-L-phenylalanine (Cbz-L-Phe)) have been investigated by X-ray crystallography. The type of β-turn present at the N-terminus and the global screw-sense preferences of the Aib foldamers were determined by analysis of intramolecular hydrogen-bonds and peptide torsion angles. The contrasting influence of a C-terminal ester or amide on the 310 helical conformation of the foldamers was established by identifying the hydrogen-bonding motifs adopted in the solid state. The ability of non-Aib achiral quaternary residues in the middle of the chain to stabilise the 310 helix was similarly confirmed. Combining these structural features, which promote the formation of consecutive i → i + 3 β-turns in Aib foldamers, permitted the formation of long chain oligomers in 310 helical conformations that extend over 21 Å.
Starting Page	3288
Ending Page	3294
Page Count	7
File Format	HTM / HTML PDF
ISSN	11440546
Volume Number	39
Issue Number	5
Journal	New Journal of Chemistry
DOI	10.1039/c4nj01547a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	X-ray crystallography N-terminus Ester Carboxylic acid 2-Aminoisobutyric acid Amide 310 helix Aib Peptide Biomolecular structure C-terminus
Content Type	Text
Resource Type	Article
Subject	Chemistry Materials Chemistry Catalysis

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