Amino Acids

, Volume 45, Issue 4, pp 957–973 | Cite as

Foldamers of β-peptides: conformational preference of peptides formed by rigid building blocks. The first MI-IR spectra of a triamide nanosystem

  • Gábor Pohl
  • Esther Gorrea
  • Vicenç Branchadell
  • Rosa M. Ortuño
  • András Perczel
  • György TarczayEmail author
Original Article


To determine local chirality driven conformational preferences of small aminocyclobutane-1-carboxylic acid derivatives, X-(ACBA) n -Y, their matrix-isolation IR spectra were recorded and analyzed. For the very first time model systems of this kind were deposited in a frozen (~10 K) noble gas matrix to reduce line width and thus, the recorded sharp vibrational lines were analyzed in details. For cis-(S,R)-1 monomer two “zigzag” conformers composed of either a six or an eight-membered H-bonded pseudo ring was identified. For trans-(S,S)-2 stereoisomer a zigzag of an eight-membered pseudo ring and a helical building unit were determined. Both findings are fully consistent with our computational results, even though the relative conformational ratios were found to vary with respect to measurements. For the dimers (S,R,S,S)-3 and (S,S,S,R)-4 as many as four different cis,trans and three different trans,cis conformers were localized in their matrix-isolation IR (MI-IR) spectra. These foldamers not only agree with the previous computational and NMR results, but also unambiguously show for the first time the presence of a structure made of a cis,trans conformer which links a “zigzag” and a helical foldamer via a bifurcated H-bond. The present work underlines the importance of MI-IR spectroscopy, applied for the first time for triamides to analyze the conformational pool of small biomolecules. We have shown that the local chirality of a β-amino acid can fully control its backbone folding preferences. Unlike proteogenic α-peptides, β- and especially (ACBA) n type oligopeptides could thus be used to rationally design and influence foldamer’s structural preferences.


β-peptides Peptide folding Matrix-isolation IR spectroscopy Conformational analysis Synthetic biopolymers 



This work was funded by the Hungarian Scientific Research Fund (OTKA K75877, K72973, NK101072), the Spanish Ministerio de Ciencia e Innovación (CTQ2010-15408/BQU) and the Generalitat de Catalunya, Spain (2009SGR-733). The European Union and the European Social Fund have provided financial support to the project under the grant no. TAMOP 4.2.1./B-09/KMR-2010-0003 and COST Action CM0803.

Conflict of interest

The authors declare that they have no competing financial interests.

Supplementary material

726_2013_1552_MOESM1_ESM.doc (1.1 mb)
Supplementary material 1 (DOC 1154 kb)


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Copyright information

© Springer-Verlag Wien 2013

Authors and Affiliations

  • Gábor Pohl
    • 1
    • 2
  • Esther Gorrea
    • 3
  • Vicenç Branchadell
    • 3
  • Rosa M. Ortuño
    • 3
  • András Perczel
    • 1
    • 2
  • György Tarczay
    • 4
    Email author
  1. 1.Laboratory of Structural Chemistry and Biology, Institute of ChemistryEötvös UniversityBudapest 112Hungary
  2. 2.Protein Modelling Group MTA-ELTE, Institute of ChemistryEötvös UniversityBudapest 112Hungary
  3. 3.Department of ChemistryUniversitat Autònoma de BarcelonaBarcelonaSpain
  4. 4.Laboratory of Molecular Spectroscopy, Institute of ChemistryEötvös UniversityBudapest 112Hungary

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