Abstract
We have analyzed a series of peptides derived from the C-terminus of alpha-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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alcohol Dehydrogenase / metabolism
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Amino Acid Sequence
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Molecular Chaperones / pharmacology*
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Molecular Sequence Data
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Monophenol Monooxygenase
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Peptide Fragments / pharmacology
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Peptides, Cyclic / pharmacology*
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Protein Denaturation / drug effects
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Thiosulfate Sulfurtransferase / pharmacology
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alpha-Synuclein / chemistry*
Substances
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Molecular Chaperones
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Peptide Fragments
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Peptides, Cyclic
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alpha-Synuclein
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Alcohol Dehydrogenase
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Monophenol Monooxygenase
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Thiosulfate Sulfurtransferase