C-9/12 Ribbon-Like Structures in Hybrid Peptides Alternating - and Thiazole-Based -Amino Acids

According to their restricted conformational freedom, heterocyclic -amino acids are usually considered to be related to Z-vinylogous -amino acids. In this context, oligomers alternating -amino acids and thiazole-based -amino acids (ATCs) were expected to fold into a canonical 12-helical shape as des...

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Published inChemistry : a European journal Vol. 23; no. 69; pp. 17584 - 17591
Main Authors Bonnel, Clement, Legrand, Baptiste, Simon, Matthieu, Martinez, Jean, Bantignies, Jean-Louis, Kang, Young Kee, Wenger, Emmanuel, Hoh, Francois, Masurier, Nicolas, Maillard, Ludovic T.
Format Journal Article
LanguageEnglish
Published WEINHEIM Wiley 11.12.2017
Subjects
Chemistry
Chemistry, Multidisciplinary
Physical Sciences
Science & Technology
HELIX FORMATION
BUILDING-BLOCKS
amino acids
SECONDARY STRUCTURES
ribbon structures
peptides
torsion angles
BETA-PEPTIDES
DENSITY FUNCTIONALS
PROTEINOGENIC SIDE-CHAINS
GAMMA-PEPTIDES
X-RAY-CRYSTAL
NMR-SOLUTION
ALPHA/GAMMA-HYBRID
structure elucidation
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Summary:According to their restricted conformational freedom, heterocyclic -amino acids are usually considered to be related to Z-vinylogous -amino acids. In this context, oligomers alternating -amino acids and thiazole-based -amino acids (ATCs) were expected to fold into a canonical 12-helical shape as described for /-hybrid peptides composed of cis-/-unsaturated -amino acids. However, through a combination of X-ray crystallography, NMR spectroscopy, FTIR experiments, and DFT calculations, it was determined that the folding behavior of ATC-containing hybrid peptides is much more complex. The homochiral /(S)-ATC sequences were unable to adopt a stable conformation, whereas the heterochiral /(R)-ATC peptides displayed novel ribbon structures stabilized by unusual C-9/12-bifurcated hydrogen bonds. These ribbon structures could be considered as a succession of pre-organized / dipeptides and may provide the basis for designing original -helix mimics.
ISSN:0947-6539
1521-3765
DOI:10.1002/chem.201704001