Cyclization of alpha-synuclein derived peptide increases its chaperone-like activity.
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.
Kim
Thomas Doohun
TD
Department Biological and Molecular Engineering, College of Engineering, Ajou University, Suwon, South Korea 443-749. doohunkim@ajou.ac.kr
D000426:Alcohol Dehydrogenase / Q000378:metabolism; D000595:Amino Acid Sequence; D018832:Molecular Chaperones / Q000494:pharmacology*; D008969:Molecular Sequence Data; D014442:Monophenol Monooxygenase; D010446:Peptide Fragments / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000494:pharmacology*; D011489:Protein Denaturation / Q000187:drug effects; D013884:Thiosulfate Sulfurtransferase / Q000494:pharmacology; D051844:alpha-Synuclein / Q000737:chemistry*
D018832:Molecular Chaperones; D010446:Peptide Fragments; D010456:Peptides, Cyclic; D051844:alpha-Synuclein; D000426:Alcohol Dehydrogenase; D014442:Monophenol Monooxygenase; D013884:Thiosulfate Sulfurtransferase