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Clinical trials targeting alpha-synuclein protein in Parkinson’s disease

Clinical trials targeting alpha-synuclein protein in Parkinson’s disease

 

Deposition of alpha-synuclein (α-synuclein) in the brain is the pathological hallmark of Parkinson’s disease (PD). There is abundant evidence that α-synuclein is not simply a marker but is essential for PD pathogenesis. Aggregates of α-synuclein, termed “Lewy bodies”, interfere with autolysosomal degradation in brain neurons and contribute to neuronal death. Therefore, α-synuclein has become a major therapeutic target in PD. Multiple clinical trials are ongoing (see below)[1].

 

Clinical Trial Phase Status Sponsor Intervention/Agent
Phase II Active Biogen BIIB054
Phase II Active Hoffmann-La Roche Prasinezumab
Phase II Active Georgetown University Nilotinib
Phase I Completed Neuropore Therapies, Inc. NPT200-11
Phase I Completed Affiris AFFITOPE PD01A and PD03A
Phase I Active University of Colorado, Denver Phenylbutyrate
Phase I Recruiting H. Lundbeck A/S Lu AF82422
Phase I Recruiting AstraZeneca MEDI1341

 

GeneTex is proud to introduce a set of active recombinant proteins, including preformed fibrils of human and mouse α-synuclein proteins and active human tau protein in fibrillar and monomeric forms. The structure of these active proteins was assessed by transmission electron microscopy (TEM), and the biological activities were tested using functional assays on cultured cells.

To view our complete catalog of active recombinant proteins, please visit our website at /Product/Overview/proteins_peptides 

Rat primary hippocampal neurons were treated with active α-synuclein protein (GTX17669-pro) and examined by immunostaining.

Rat primary hippocampal neurons were treated with active α-synuclein protein (GTX17669-pro) and examined by immunostaining.
 
Rat primary hippocampal neurons demonstrate Lewy body inclusion formation when treated with active mouse a-synuclein protein preformed fibrils (GTX17671-pro).

Rat primary hippocampal neurons demonstrate Lewy body inclusion formation when treated with active mouse a-synuclein protein preformed fibrils (GTX17671-pro).
 
TEM of human tau (K18) protein, mutant P301L (active, preformed fibrils) (GTX17675-pro) shows typical fibrillar structure.

TEM of human tau (K18) protein, mutant P301L (active, preformed fibrils) (GTX17675-pro) shows typical fibrillar structure.
 
Thioflavin T emission curves show increased fluorescence (correlating with tau aggregation) in tau K18 P301L monomers (GTX17673-pro) over time.

Thioflavin T emission curves show increased fluorescence (correlating with tau aggregation) in tau K18 P301L monomers (GTX17673-pro) over time.
 

References:

  1. Clinical Trial Highlights: Targetting Alpha-Synuclein.