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A readily applicable strategy to convert peptides to peptoid-based therapeutics.


ABSTRACT: Incorporation of unnatural amino acids and peptidomimetic residues into therapeutic peptides is highly efficacious and commonly employed, but generally requires laborious trial-and-error approaches. Previously, we demonstrated that C20 peptide has the potential to be a potential antiviral agent. Herein we report our attempt to improve the biological properties of this peptide by introducing peptidomimetics. Through combined alanine, proline, and sarcosine scans coupled with a competitive fluorescence polarization assay developed for identifying antiviral peptides, we enabled to pinpoint peptoid-tolerant peptide residues within C20 peptide. The synergistic benefits of combining these (and other) commonly employed methods could lead to a easily applicable strategy for designing and refining therapeutically-attractive peptidomimetics.

SUBMITTER: Park M 

PROVIDER: S-EPMC3605428 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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A readily applicable strategy to convert peptides to peptoid-based therapeutics.

Park Minyoung M   Wetzler Modi M   Jardetzky Theodore S TS   Barron Annelise E AE  

PloS one 20130321 3


Incorporation of unnatural amino acids and peptidomimetic residues into therapeutic peptides is highly efficacious and commonly employed, but generally requires laborious trial-and-error approaches. Previously, we demonstrated that C20 peptide has the potential to be a potential antiviral agent. Herein we report our attempt to improve the biological properties of this peptide by introducing peptidomimetics. Through combined alanine, proline, and sarcosine scans coupled with a competitive fluores  ...[more]

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