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1. Chiappori F, Ferrario MG, Gaiji N, Fantucci P Docking of estrogen and genistein like molecular library on Estrogen Receptor alpha and beta Meeting: BITS 2005 - Year: 2005 Full text in a new tab Topic: Unspecified Abstract: Estrogen replacement therapy is one of the most efficient treatment of menopausal symptoms. Unfortunately, despite the benefits of estrogenic therapy evidence exists of increasing number of cases of reproductive tissue cancer. This lead to a strong interest in discovering new compounds that display the benefits of estrogens avoiding such risks. We decided to apply a virtual high throughput screening, based on docking simulations, for the identification of new possible selective receptor compounds. |
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2. Chiappori F, Ferrario MG, Gaiji N, Fantucci P Design of Selective Compounds for the Estrogen Receptors: A Molecular Docking and Machine Learning Study Meeting: BITS 2006 - Year: 2006 Full text in a new tab Topic: Combinatorial libraries and drug design Abstract: Missing |
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3. Ferrario MG, Chiappori F, Ferrario MG, Gaiji N, Fantucci P Molecular dynamic study of the ligand binding domain of estrogen receptor alfa and beta Meeting: BITS 2005 - Year: 2005 Full text in a new tab Topic: Unspecified Abstract: Estrogen Receptor belongs to the Nuclear receptor family, there are two different currently known subtypes Era and Erb. Levels and proportion of the two subtypes differs in different target cells. We can hypotheses a different pharmacological activity upon ligand binding. The aim of this work is the investigation through molecular dynamics simulations, on both the subtypes a and b of the estrogen receptor, of possible differences among them and for the study of their dynamical behaviour. |
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4. Ferrario MG, Chiappori F, Gaiji N, Fantucci P Alpha and Beta Estrogen Receptors: Molecular Modelling and Conformational Analysis through Molecular Dynamics Meeting: BITS 2006 - Year: 2006 Full text in a new tab Topic: Protein structure Abstract: Missing |
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5. Gaiji N, Mazzitello R, Beringhelli T, Fantucci P Bovine β-lactoglobulin: Interaction studies with Norfloxacin Meeting: BITS 2004 - Year: 2004 Full text in a new tab Topic: Unspecified Abstract: Molecular docking is an efficient computational tool to predict the structures of protein-ligand complex. This kind of simulation is of fundamental importance for interpretation of numerous biochemical phenomena, providing useful information on the preferred binding sites of ligands, and therefore in rational drug design. Bovine β-lactoglobulin (BLG) is a small extracellular protein belonging to the lipocalin superfamily. Lipocalins have been classified as transport proteins with the remarkable ability of binding small hydrophobic molecules within the central cavity also known as calyx. Because of its stability, abundance and easiness of preparation BLG, has been frequently studied to clarify its structural and binding features. Several studies suggest that more than one binding site exists, thus the aim of this work is to investigate the existence of other sites, in addition to the calyx one, and to verify if BLG can interact and play the role of carrier of drugs. We considered the particular case of Norfloxacin which is a broad-spectrum antibiotic used in treatment of urinary tract infections. |