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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 ordered nanostructures, a key process that is central for many physiological features such as night vision in mammals and reptiles, and camouflage of chameleons, but also underlying the pathophysiology of various age-related and newborn disorders. We adopted a unique and original reductionist approach to determine the minimal modules that facilitate the molecular recognition and self-assembly processes driving the formation of ordered nanostructures in physiology, pathology, and nanotechnology. Most importantly, we use tools from chemistry, physics, and materials science to understand basic phenomena in biology. ​
AMYLOID FIBRIL FORMATION
A major interest in the lab is concerned with 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 worldwide, such as Alzheimer's disease, Parkinson's disease, and Type II Diabetes. 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. We also study the cross-talk between amyloids and the metabolome to understand the predisposition to be affected by these disorders.
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 a casting mold for the fabrication of metallic nano-wires and coaxial nano-cables. We had used inkjet technology as well as vapor 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 unique physical properties of the nanostructure include mechanical, electronic, piezoelectric, and nonlinear optical ones. We recently discovered the ability of peptides also to form an amorphous self-healing glass that is transparent in the visible and infrared.
​METABOLITE AMYLOIDS
More than a decade ago, 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 the disease phenotype. We use yeast and nematode models to study these diseases.
