Cyclization of α-Synuclein Derived Peptide Increases Its Chaperone-Like Activity

Thomas   D.   Kim

doi:10.2174/092986606775974438

Abstract

We have analyzed a series of peptides derived from the C-terminus of α-synuclein for chaperone-like activity. Specifically, a cyclic peptide generated by introducing a disulfide bond was observed to increase chaperone-like activity. This is the first example of a disulfide-crosslinked peptide that exhibits activity against protein aggregation and activity loss.

Keywords: α-Synuclein, chaperone-like activity, protective molecule, aggregation

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Protein & Peptide Letters

Title: Cyclization of α-Synuclein Derived Peptide Increases Its Chaperone-Like Activity

Volume: 13 Issue: 4

Author(s): Thomas D. Kim

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Keywords: α-Synuclein, chaperone-like activity, protective molecule, aggregation

Abstract: We have analyzed a series of peptides derived from the C-terminus of α-synuclein for chaperone-like activity. Specifically, a cyclic peptide generated by introducing a disulfide bond was observed to increase chaperone-like activity. This is the first example of a disulfide-crosslinked peptide that exhibits activity against protein aggregation and activity loss.

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Kim D. Thomas, Cyclization of α-Synuclein Derived Peptide Increases Its Chaperone-Like Activity, Protein & Peptide Letters 2006; 13 (4) . https://dx.doi.org/10.2174/092986606775974438