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Computational design of a self-assembling ?-peptide oligomer.

ABSTRACT: The first computationally designed self-assembling oligomer consisting of exclusively ?-amino acids (?AAs) is presented. The packing of a ?-3(14) helix into coiled-coils of varying stoichiometries as a function of amino acid sequence is examined. ?-Peptides with hVal repeating every third residue in the sequence appeared to have a strong propensity to pack into hexameric bundles. The designed sequence was synthesized and characterized with CD spectroscopy, NMR, and analytical ultracentrifugation, suggesting that the peptide adopts a well-folded hexameric structure.

SUBMITTER: Korendovych IV 

PROVIDER: S-EPMC3807245 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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Computational design of a self-assembling β-peptide oligomer.

Korendovych Ivan V IV   Kim Yong Ho YH   Ryan Andrew H AH   Lear James D JD   Degrado William F WF   Shandler Scott J SJ  

Organic letters 20101014 22

The first computationally designed self-assembling oligomer consisting of exclusively β-amino acids (βAAs) is presented. The packing of a β-3(14) helix into coiled-coils of varying stoichiometries as a function of amino acid sequence is examined. β-Peptides with hVal repeating every third residue in the sequence appeared to have a strong propensity to pack into hexameric bundles. The designed sequence was synthesized and characterized with CD spectroscopy, NMR, and analytical ultracentrifugation  ...[more]