Heterotypic interactions with Aβ42 reshape α-syn aggregation pathways and fibril conformations, generating structurally distinct α-syn fibril populations with different neuronal seeding activities, which provide a molecular framework for understanding how cross-talk between amyloidogenic proteins may contribute to structural and pathological heterogeneity in mixed neurodegenerative diseases.
Parkinson’s disease (PD) is a severe, progressive neurodegenerative disorder characterized by aggregation of the protein α-synuclein into amyloid fibrils, leading to the formation of Lewy bodies and Lewy neurites and degeneration of dopaminergic neurons in the substantia nigra. Although α-synuclein aggregation is a def...
Parkinson's disease (PD) is characterized by the pathological aggregation of α-synuclein (α-syn) into β-sheet-rich fibrils, contributing to neuronal toxicity and oxidative stress. In this study, we investigated the inhibitory and disaggregating effects of Triprolidine (TC) on α-syn fibrillation through a combined exper...
Md Nadir Hassan, Murtaza Hussain, Faisal Nabi et al.· Biochemistry· 0 citations
Based on the structure, a DJ-1-derived peptide (173-180) is designed that significantly inhibited α-synuclein aggregation in TEM and ELISA assays, suggesting its potential as a therapeutic candidate for α-synucleinopathies.
Hyeon Jin Kim, Da Hye Kim, Chang-Woo Han et al.· International Journal of Bio...· 0 citations
The Affinity-directed PROtein Missile system is employed and targeted degradation of α-synuclein impedes the pre-formed fibril (PFF)-induced aggregation of α-synuclein in primary neurons derived from rats expressing human α-synuclein.
Bill Carton, Géraldine Gelders, Gajanan Sathe et al.· npj Parkinson's Disease· 0 citations
The non-amyloid-β component (NAC) region of the Parkinson’s-associated protein α-synuclein plays a key role in its pathogenic aggregation, motivating the development of molecules that target this critical region. Here, we show that a minimal NAC-derived motif, 66VGGAVVT72, can be reprogrammed through backbone engineeri...
Haoliang Zheng, Kyren Miller, Magdalena I. Ivanova et al.· bioRxiv· 0 citations
The pathological aggregation of α-synuclein (α-syn), an intrinsically disordered protein that regulates synaptic vesicle trafficking in the brain, is a defining molecular feature in Parkinson’s disease (PD). Early oligomeric assemblies are widely considered the most neurotoxic species, yet their structural features rem...
Raya Sadighi, Andrea Istrati, Sigourney Karijodikoro et al.· ACS Central Science· 1 citation
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