ArticleThe Journal of biological chemistry2015
Intracellular screening of a peptide library to derive a potent peptide inhibitor of α-synuclein aggregation.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Protein Recognition of Linear and Cyclic Peptides of Homologous Sequences Implicated in the Aggregation of α-Synuclein.The journal of physical chemistry. B · 2025Article
- Article
- Using a stable protein scaffold to display peptides that bind to alpha-synuclein fibrils.Protein science : a publication of the Protein Society · 2025Article
- Rapid discovery of cyclic peptide protein aggregation inhibitors by continuous selection.Nature chemical biology · 2025Article
- Peptide-based approaches to directly target alpha-synuclein in Parkinson's disease.Molecular neurodegeneration · 2023Review
- Development of a hydroxyflavone-labelled 4554W peptide probe for monitoring αS aggregation.Scientific reports · 2023Article
- Defensin-based therapeutic peptide design in attenuating V30M TTR-induced Familial Amyloid Polyneuropathy.3 Biotech · 2023Article
- Disrupting the α-synuclein-ESCRT interaction with a peptide inhibitor mitigates neurodegeneration in preclinical models of Parkinson's disease.Nature communications · 2023Article
- Peptide-based LDH5 inhibitors enter cancer cells and impair proliferation.Cellular and molecular life sciences : CMLS · 2022Article
- Library-Derived Peptide Aggregation Modulators of Parkinson's Disease Early-Onset α-Synuclein Variants.ACS chemical neuroscience · 2022Article
- miRNA and antisense oligonucleotide-based α-synuclein targeting as disease-modifying therapeutics in Parkinson's disease.Frontiers in pharmacology · 2022Review
- Natural Alkaloid Compounds as Inhibitors for Alpha-Synuclein Seeded Fibril Formation and Toxicity.Molecules (Basel, Switzerland) · 2021Article
- Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation.Frontiers in molecular neuroscience · 2021Article
- Using protein engineering to understand and modulate aggregation.Current opinion in structural biology · 2020Review
- Insights Into Peptide Inhibition of Alpha-Synuclein Aggregation.Frontiers in neuroscience · 2020Article
- Characterizing the inhibition of α-synuclein oligomerization by a pharmacological chaperone that prevents prion formation by the protein PrP.Protein science : a publication of the Protein Society · 2019Article
- Alpha-synuclein structure and Parkinson's disease - lessons and emerging principles.Molecular neurodegeneration · 2019Review
- Unbiased Screens for Modifiers of Alpha-Synuclein Toxicity.Current neurology and neuroscience reports · 2019Review
- Small molecule probes of protein aggregation.Current opinion in chemical biology · 2017Review
- An enhanced recombinant amino-terminal acetylation system and novel in vivo high-throughput screen for molecules affecting α-synuclein oligomerisation.FEBS letters · 2017Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Aggregation of α-synuclein (α-syn) into toxic fibrils is a pathogenic hallmark of Parkinson disease (PD). Studies have focused largely on residues 71-82, yet most early-onset mutations are located between residues 46 and 53. A semirationally designed 209,952-member library based entirely on this region was constructed, containing all wild-type residues and changes associated with early-onset PD. Intracellular cell survival screening and growth competition isolated a 10-residue peptide antagonist that potently inhibits α-syn aggregation and associated toxicity at a 1:1 stoichiometry. This was verified using continuous growth measurements and 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide cytotoxicity studies. Atomic force microscopy and circular dichroism on the same samples showed a random-coil structure and no oligomers. A new region of α-syn for inhibitor targeting has been highlighted, together with the approach of using a semirational design and intracellular screening. The peptides can then be used as candidates for modification in drugs capable of slowing or even preventing the onset of PD.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.