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Research
MOLECULAR SELF-ASSEMBLY
AMYLOID FIBRIL FORMATION
NANOBIOTECHNOLOGY
METABOLITE AMYLOIDS
MOLECULAR SELF-ASSEMBLY
We study one of the most important problems in contemporary life sciences and medicine: Understanding the molecular basis for the formation of amyloid nanostructures in degenerative disorders, a process underlying the pathophysiology of some of the most devastating health problems world-wide, such as Alzheimer's disease, Parkinson's disease and Diabetes Mellitus type II. We adopted a unique and original reductionist approach to determine the minimal modules that facilitate the molecular recognition and self-assembly processes driving amyloid fibril formation in largely all known amyloidogenic proteins.​
AMYLOID FIBRIL FORMATION
We study one of the most important problems in contemporary life sciences and medicine: Understanding the molecular basis for the formation of amyloid nanostructures in degenerative disorders, a process underlying the pathophysiology of some of the most devastating health problems world-wide, such as Alzheimer's disease, Parkinson's disease and Diabetes Mellitus type II. We adopted a unique and original reductionist approach to determine the minimal modules that facilitate the molecular recognition and self-assembly processes driving amyloid fibril formation in largely all known amyloidogenic proteins.
NANOBIOTECHNOLOGY
We revealed the ability of the aromatic diphenylalanine peptide to form hollow nanotubes with remarkable persistence length. We demonstrated the ability to use these peptide nanostructures as casting mould for the fabrication of metallic nano-wires and coaxial nano-cables. We had used inkjet technology as well as vapour deposition methods to coat surfaces and form peptide “nano-forests” in a highly controlled manner. We demonstrated that other aromatic homodipeptides could self-assemble to form nanospheres, nanoplates, nanofibrils and hydrogels with nanoscale order. These various assemblies are being formed by remarkably simple building blocks that have the potential to be synthesized in large amounts at a low cost. The nanostructures properties include ultra-rigidity, semi-conductive, piezoelectric and non-linear optics properties.
​METABOLITE AMYLOIDS
In recent years, we realized that the amyloid hypothesis could be extended to include amyloid-like structures based on single metabolites. Employing our minimalist-reductionist approach, we have been able to show that single amino-acids, nucleobases and other metabolites can self-assemble to form ordered structures exhibiting similar characteristics to those of protein amyloids. Our studies suggest that these metabolite-amyloids may be involved in the pathogenesis and progression of Inborn Error of Metabolism (IEM) disorders, such as Phenylketonuria (PKU). Current efforts are invested in further characterizing metabolite-amyloids, utilizing a variety of models, and their link to disease. In addition, we are exploring possible therapeutic avenues for IEMs based on small molecules that interfere with the amyloid-like structures and thus alleviate disease phenotype.
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