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| Guido Tiana, University of Milan |
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| Guido Tiana graduated in Physics at the University of Milano (Italy) and obtained his Ph.D. at the Niels Bohr Institute of Copenhagen (Denmark). He also spent some time at the Centre for Biological Sequence Analysis (Lyngby, Denmark) and at the Department of Chemistry and Biological Chemistry at Harvard University. He is currently a researcher at the Department of Physics of the University of Milano. He is interested in the physics of biological systems, particularly of the folding of proteins, but also of protein evolution, genetic networks and protein-DNA interaction.
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Design of a folding inhibitor of the HIV-1 Protease
Guido Tiana, University of Milan
HIV-1 Protease is an essential enzyme in the viral life cycle of the HIV-1 virus. Because the stability of single domain proteins, like each of the monomers of HIV-1-PR, is controlled by a core built out of short, strongly interacting fragments of the protein (Local Elementary Structures, or LES) which have evolved over myriads of generations to recognize and strongly attract each other, we suggest a novel type of HIV-1-PR inhibitors: short peptides displaying the same amino acid sequence of that of a LES. In particular, we identify a peptide displaying a sequence identical to that of the stretch comprising amino acids 83-93 of the HIV-1-PR monomer. This peptide is expected not to develop resistance, because mutations in the stabilization core of the protein, which decrease the affinity with the peptide, are also likely to destabilize consistently the protein. We make use of a simplified model to show the efficiency and specificity of this inhibitor.
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