Leuven researchers have deployed synthetic amyloids to trigger protein misfolding as a strategy to combat the influenza A and Zika virus.
Chaperones are essential for proper protein folding. Understanding the biological principles of chaperone-protein binding can help prevent toxic protein aggregation, which occurs in a wide range of disorders. A Leuven research team now shows how the preference of chaperones for basic residues came about.
On November 6, VIB and KU Leuven opened the NextGenQBio platform. This state-of-the-art project was granted to VIB and the Stem Cell Institute Leuven (SCIL) within the purview of the Hercules Foundation financing for large scale research infrastructure.
Catching tumors in a spider’s web’: that metaphor was used by Joost Schymkowitz and Frederic Rousseau (both VIB-KU Leuven Center for Brain & Disease Research) in a 2016 press release following a Science publication on their peptide-based protein knockdown technology. Fast forward to 2018: our 20th spin-off Aelin Therapeutics has just been launched, and Joost and Frederic’s coveted technology platform is now up and running.
Aelin Therapeutics, a privately held Belgian biotherapeutics company, announces today that it has secured a 27 M€ investment to pioneer a novel modality in drug development in order to create a completely new class of antibiotics and first-in-class therapeutics against high-value undruggable human targets. The technology, branded Pept-ins™, harnesses the power of protein aggregation to specifically induce functional knockdown of a target protein. The company will use the proceeds of the 27 M€ Series A financing, to bring a first Pept-in product to the clinic.
The ERC Proof of Concept Grants are awarded to recent winners of ERC grants working on high-potential research projects to bridge the chasm between scientific exploration and commercial innovation. Joost Schymkowitz (Switch Lab, VIB-KU Leuven Center for Brain & Disease Research) recently obtained a POC ERC of 150 000Euro grant.
Boiled eggs, beer foam and spider silk might seem unrelated at first glance. However, their proteins all share a similar structural element: amyloid. Although these ‘clumps’ of proteins are usually associated with disease development, their properties could be used to fight a wide array of conditions. Enter Pept-inTM: a brand-new technology platform that exploits the power of protein aggregation to develop novel medicines. Credits go to our Switch Laboratory (VIB-KU Leuven) and inventors Frederic Rousseau and Joost Schymkowitz (VIB-KU Leuven).
After a decade of research, the Belgian Switch Laboratory (VIB/KU Leuven) has revealed a new designer molecule that inhibits a well-validated cancer driver through the mechanism of amyloid formation. This work demonstrates that amyloid structures can be used to rationally develop a novel class of biotechnological molecules that are able to fight a wide array of diseases. After the publication of this research in the leading journal Science, next steps to translate this groundbreaking technology, branded Pept-inTM into direct benefits for patients are already being explored by VIB.
Natural selection results in protein sequences that are only soluble to the level that is required to carry out its physiological function. However, in biotechnological applications, we need these proteins to survive concentrations that are up to 1000-fold higher that what naturally occurs, e.g. an antibody drug in the syringe prior to injection. Moreover, these proteins are isolated at high purity and can thus no longer count on the help of molecular chaperones that all living organisms employ to keep its proteins in shape. As a result, biotechnological and therapeutic applications of protein are often hampered or rendered impossible by the mismatch between the natural solubility of a protein and the requirements of the application. This raises the question whether the solubility of natural protein sequences could be improved without affecting their intended function.
Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are two devastating adult-onset neurodegenerative disorders. No cure exists for these diseases. Ten percent of ALS patients suffer from a familial form of the disease, while FTD is caused in 40% of patients by a genetic defect. In 2011, the most important genetic cause of ALS and FTD was discovered. The causative mutation was a repetition of a piece of non-coding DNA, a so called tandem repeat, in a gene with an unknown function, named C9orf72. A team of scientists from VIB and KU Leuven now discovered that proteins translated from this tandem repeat interfere with the nucleocytoplasmic transport which they found is essential for causing ALS and FTD.