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MMBio - Marie Curie Training Network

Valerio Viali

 
Valerio_Viali_153
 

Background:
I graduated cum laude in Industrial Chemistry at the University of Rome “La Sapienza” January 2017 and I did an Erasmus+Traineeship experience in the University of Bordeaux from March to August.
During my thesis work I have been involved in a project concerning the synthesis and the characterization of NPs, given by self-assembling of hybrid conjugate peptide-PEG, as drug delivery systems. As the conjugate was obtained by Solid Phase Synthesis, the morphology and the drug delivery properties of the NPs were studied by UV, Fluorescence, Circular Dichroism and NMR spectroscopy.
My studies in the University of Bordeaux were focused on Foldamers, in particular Chimeras, conjugate peptide-oligoureas that are able to give proteins-like quaternary structures in aqueous phase. This work, whose aim was de novo design of enzyme mimic using helical bundles, was divided into two main modules: the organic synthesis of both the urea building blocks and the chimeras, and the characterization of the latter aggregative properties using Electrospray Ionization Ion Mobility Spectrometry (ESI-IMS) and, ones they are obtained as crystal, X-rays Diffraction.

Training and Transferable Skills:

- Solid Phase Organic Chemistry

- Multistep organic synthesis

- Preparative and analytical HPLC

- NMR, IR, UV-Vis and Fluorescence Spectroscopy

- ES-MS

- Crystallography (hanging drop vapor diffusion technique)

Research Projects:
My Ph.D. project aims to create RNA/DNA cleaving agents capable of highly localised activity. Such molecules can have numerous applications as versatile replacements for nucleases laboratory tools and therapeutic agent against cancer, bacteria and viruses. More fundamentally, studying artificial systems both tests and expands our understanding of how catalysis works under biological conditions. The project concerns both synthesis to create ligands, complexes and substrates, and practical and intellectual analysis to understand how the catalysts we design work. Enzymes and ribozymes that catalyze the hydrolysis of phosphate esters frequently utilize metal ion cofactors in a central catalytic role, and for this reason many studies have focused on the synthesis of metal-ion complexes. Because the high stability of the RNA and DNA, creating efficient artificial catalysts that can compete with biocatalysis is challenging and in order to enhance the activity is necessary to well design the structure.
As double metal ion systems are involved in many biological systems, to achieve that one of the main strategies concern the use of di or polynuclear metal complexes. Also in nature, many metalloenzymes that catalyse phosphate ester cleavage use amino acid side chains to enhance the activity; for this reason, the project will be focused on the design of more powerful catalysts able to provide hydrogen bond donors that are rigidly preorganized to interact with the substrate coordinated to the zinc ion.

 

 

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