Helix foldamers of γ-peptides based on 2-aminocyclopentylacetic acidElectronic supplementary information (ESI) available: Backbone torsion angles of optimized helical and extended structures of oligo-γAc5a peptides, mean distances and angles for H-bonds of helix foldamers, helical parameters of helix foldamers, optimized helical and extended structures and Cartesian coordinates of oligo-γAc5a peptides. See DOI: 10.1039/c4nj01202j
The conformational preferences of helix foldamers have been studied in oligo-γ-peptides composed of 2-aminocyclopentylacetic acid (γAc 5 a) with a cyclopentyl constraint on the C β -C γ bond using density functional methods. Although the γAc 5 a ( 1 ) dipeptide with homochiral (1 S ,2 S ) configurat...
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Main Authors | , |
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Format | Journal Article |
Language | English |
Published |
06.05.2015
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Online Access | Get full text |
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Summary: | The conformational preferences of helix foldamers have been studied in oligo-γ-peptides composed of 2-aminocyclopentylacetic acid (γAc
5
a) with a cyclopentyl constraint on the C
β
-C
γ
bond using density functional methods. Although the γAc
5
a (
1
) dipeptide with homochiral (1
S
,2
S
) configurations exhibits a strong preference for the right-handed (
P
) 9-membered helix foldamer in chloroform and water, oligopeptides composed of γAc
5
a (
1
) preferentially adopt (
P
)-2.5
14
-helices due to the favored conformational energy produced as the peptide sequence becomes longer and as solvent polarity increases. The calculated mean backbone torsion angles and helical parameters for 14-helical foldamers composed of γAc
5
a (
1
) are consistent with those measured in the X-ray structures of penta- and hexapeptides composed of C
α
-ethyl-γAc
6
a and 14-helical foldamers composed of γAc
6
a (
1
) with cyclohexyl constraints. However, the substitution of cyclopentane constraints in the backbone differentially changed the conformational preference and/or handedness for helix foldamers when compared with other oligo-γ-peptides with different cycloalkane positions or size constraints. The conformational preferences of the oligo-γAc
5
a peptides obtained here are expected to provide useful information for the structure-based design of biologically active γ-peptides with specific functions.
Oligo-γ-peptides based on 2-aminocyclopentylacetic acid (γAc
5
a) with a cyclopentyl constraint on the C
β
-C
γ
bond and homochiral (1
S
,2
S
) configurations preferentially adopt the right-handed 14-helix foldamers in the gas phase and in solution. |
---|---|
Bibliography: | 10.1039/c4nj01202j 5 Electronic supplementary information (ESI) available: Backbone torsion angles of optimized helical and extended structures of oligo-γAc a peptides, mean distances and angles for H-bonds of helix foldamers, helical parameters of helix foldamers, optimized helical and extended structures and Cartesian coordinates of oligo-γAc a peptides. See DOI |
ISSN: | 1144-0546 1369-9261 |
DOI: | 10.1039/c4nj01202j |