Extended apolar β-peptide foldamers: The role of axis chirality on β-peptide sheet stability

Gábor Pohl, Tamás Beke, I. Csizmadia, A. Perczel

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

This study is on structure and stability of sheetlike conformers of β-peptides; never seen new foldamers are reported here for the first time. Single- and double-stranded structures are analyzed, and the seeds of large β-layers and biocompatible nanomaterials are described here. Both the monomeric, HCO-[NH-CH2-CH2CO]n-NH2, and dimeric forms, [HCO-(β-Ala)n-NH2]2 n = 3 and 4, of oligo-β-alanine supramolecular complexes are evaluated by using an adequate level of theory M052X/6-31G(d) for peptides of this size. Polymers composed of backbone foldamers with the central μ torsion angle set to an anti orientation were all probed. Sheet structures built up of strands with carbonyl groups monotonically facing the same spatial direction, polar strands, were previously assigned and synthesized (Seebach, D. Chem. Biodiversity 2004, 1, 1111 -1239). Now we are presenting a novel β-peptide sheet structure of alternating carbonyl group orientations, called as apolar strands. These novel secondary structural elements of β-peptides are structural analogs of β-pleated sheets of proteins. Interestingly enough, the latter type of apolar strands are foreseen as very stable supramolecular complexes and are more firm by ∼10 kcalmol-1 than the aforementioned polar strands. Furthermore, apolar strands lack the inherent twisting of β-layers, present in polar strands resulting in the tubular shape. Once the effect of substitution of Hβ1 and/or Hβ2 atoms are revealed on foldamer stability, short peptide sequence could be designed and synthesized. These new, conformationally optimized β-sheetlike nanostructures of increased stability with little or no twisting could be used as enzymatically resistant (Frackenpohl, J., Arvidsson, P. I., Schreiber, J. V., and Seebach, D. ChemBioChem 2001, 2, 445-455) biomaterials. These newly designed models systems could enlarge the arsenal of durable polyesters of similar chemical constitution (e.g., -[O-CH(CH3)-CH 2CO]n- and -[O-CH(COOH)-CH2CO]n-) already used as artificial heart valves, for example.

Original languageEnglish
Pages (from-to)9338-9348
Number of pages11
JournalJournal of Physical Chemistry B
Volume114
Issue number29
DOIs
Publication statusPublished - Jul 29 2010

Fingerprint

Chirality
chirality
strands
Peptides
peptides
twisting
methylidyne
Arsenals
Artificial heart
Polyesters
artificial heart valves
Biodiversity
Biocompatible Materials
Nanostructured materials
Biomaterials
biological diversity
Alanine
Torsional stress
Seed
Nanostructures

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

Cite this

Extended apolar β-peptide foldamers : The role of axis chirality on β-peptide sheet stability. / Pohl, Gábor; Beke, Tamás; Csizmadia, I.; Perczel, A.

In: Journal of Physical Chemistry B, Vol. 114, No. 29, 29.07.2010, p. 9338-9348.

Research output: Contribution to journalArticle

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