α-Synuclein (61-75) is a peptide fragment derived from the larger protein α-Synuclein. α-Synuclein is predominantly found in presynaptic nerve terminals and is considered to be a biomarker candidate for Parkinson's disease (PD).

α-Synuclein (61-95) (human) constitutes the hydrophobic core of α-synuclein and is implicated in inducing neuronal cell death. This segment is utilized in the study of neurodegenerative conditions such as Alzheimer's disease (AD) and Parkinson's disease (PD) [1] [2].

α-Synuclein (61-75) TFA is a fragment (residues 61-75) of the abundant neuronal protein α-Synuclein, which is predominantly located in presynaptic nerve terminals. α-Synuclein serves as a potential biomarker for Parkinson's disease (PD) [1] [2].

α-Synuclein 4554W, previously identified through intracellular library screening, is an inhibitor of α-Synuclein (aSyn) aggregation and its associated toxicity. This compound, comprising GIVNGVKA sequences, effectively reduces fibril formation in aSyn mutants associated with Parkinson’s disease [1].

Tat-βsyn-degron, an α-synuclein knockdown peptide, integrates three domains: the HIV-1 Tat plasma membrane transduction domain, an α-synuclein binding domain (βsyn) representing amino acids 36-45 of β-synuclein, and a proteasomal targeting domain (degron). It effectively binds to recombinant α-synuclein, demonstrating a significant reduction in α-synuclein levels in primary rat cortical neuron cultures.

The compound 4A7C-301-Nurr1 agonist is a specific agonist for the nuclear receptor-related 1 (Nurr1). By binding to the Nurr1 ligand-binding domain with an IC50 value of 48.22 nM, it enhances the transcriptional activity of both Nurr1-LBD and the full-length Nurr1, as demonstrated in reporter assays using SK-N-BE(2)C human neuroblastoma cells, with EC50 values of 6.53 and 50-70 µM, respectively. Additionally, administration of 4A7C-301-Nurr1 agonist at a dosage of 5 mg/kg per day has been shown to mitigate dopaminergic cell death in the striatum and substantia nigra pars compacta and ameliorate motor and olfactory deficits in mouse models of Parkinson's disease, circumventing the induction of dyskinesia-like behaviors. These models were induced either by the neurotoxin MPTP or by overexpression of α-synuclein.