This week, because April 11 is World Parkinson’s Day, we chat with Dieter Willbold, CSO of Priavoid, and Antje Willuweit, director preclinical development of Priavoid, and we have a conversation with Karsten Eastman, CEO and co-founder of Sethera Therapeutics, about the company’s work on peptides.
Times:
02:52 Sethera Therapeutics
22:35 Priavoid
Priavoid
Priavoid, a company advancing novel disease-modifying approaches for neurodegenerative disorders, recently presented preclinical proof-of-concept data for its candidate PRI-101 in Parkinson’s disease (PD) and related synucleinopathies.
The results show that PRI-101 inhibited aggregation of α-synuclein (α-syn) and actively disassembled α-syn-fibrils across in vitro and in vivo models relevant to PD. α-syn aggregates play a key role in the disease pathology of Parkinson’s, multiple system atrophy (MSA), and other synucleinopathies.
In PD mouse models, PRI-101 was associated with prolonged median survival versus placebo. Short- and long-term treatment also led to a dose-dependent reduction of α-syn aggregates in the brain, accompanied by significant improvements in behavioural performance.
PRI-101 is orally available all-d-peptide candidate based on Priavoid’s proprietary detangler platform. By binding to α-syn, PRI-101 aims to promote the conversion of the toxic and self-replicating neurodegenerative aggregates back towards native, non-toxic α-syn-monomers, thereby counteracting disease-driving aggregation processes.
Sethera Therapeutics
A team of researchers from the University of Utah and Sethera Therapeutics have uncovered a new way to build more stable and drug-like peptides, opening the door to medicines that could target diseases long considered “undruggable.”
The team studied a natural enzyme, PapB, that can ‘staple’ peptides into circular structures known as macrocycles. What makes PapB so unusual is that it combines flexibility and precision: it works on many different building blocks—including those that biology usually rejects—yet still creates a single, predictable bond. In a single gentle step, it transforms linear peptides into sturdy, ring-shaped molecules that are more stable, more resistant to degradation, and better suited for drug development.
Many peptide drugs are stabilized with disulfide bonds, which break down in the body, or rely on complicated, costly, and time-consuming chemical methods to achieve the same effect.
PapB streamlines the process, creating durable “stapled” peptides that drug developers can program with unprecedented ease. This opens vast new chemical space for peptide medicines, including scaffolds associated with better cell penetration and oral dosing—two qualities essential for advancing peptide therapeutics.
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