Sheila J. Sadeghi

ORCID: 0000-0003-4951-1242
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About
Contact & Profiles
Research Areas
  • Pharmacogenetics and Drug Metabolism
  • Electrochemical sensors and biosensors
  • Electrochemical Analysis and Applications
  • Advanced biosensing and bioanalysis techniques
  • Computational Drug Discovery Methods
  • Enzyme Catalysis and Immobilization
  • Metal-Catalyzed Oxygenation Mechanisms
  • Analytical Chemistry and Chromatography
  • Analytical Chemistry and Sensors
  • Innovative Microfluidic and Catalytic Techniques Innovation
  • Metabolomics and Mass Spectrometry Studies
  • Microbial bioremediation and biosurfactants
  • Photosynthetic Processes and Mechanisms
  • Molecular Junctions and Nanostructures
  • Drug Transport and Resistance Mechanisms
  • Metalloenzymes and iron-sulfur proteins
  • Enzyme-mediated dye degradation
  • Microbial Metabolic Engineering and Bioproduction
  • Enzyme Structure and Function
  • Protein Structure and Dynamics
  • Electrocatalysts for Energy Conversion
  • Biotin and Related Studies
  • bioluminescence and chemiluminescence research
  • Ubiquitin and proteasome pathways
  • Protein Degradation and Inhibitors

University of Turin
2015-2025

Accademia Albertina delle Belle Arti
2013-2024

Torino e-district
2019

In-Q-Tel
2011

Imperial College London
1997-2010

GlaxoSmithKline (United Kingdom)
2010

University of California, San Francisco
2004-2008

Università degli Studi della Tuscia
2008

National Interuniversity Consortium for the Physical Sciences of Matter
2008

University of California San Francisco Medical Center
2004

We have investigated the use of optically transparent, nanoporous TiO2 films as substrates for protein immobilization. Immobilization on such may be readily achieved from aqueous solutions at 4 °C. The structure film greatly enhances active surface area available binding (by a factor 150 4-μm-thick film). demonstrate that redox state immobilized cytochrome c modulated by application an electrical bias potential to and fluorescence yield fluorophore-labeled maltose-binding used monitor...

10.1021/ac980764l article EN Analytical Chemistry 1998-10-22

Multilayer lipid membranes perform many important functions in biology, such as electrical isolation (myelination of axons), increased surface area for biocatalytic purposes (thylakoid grana and mitochondrial cristae), sequential processing (golgi cisternae). Here we develop a simple layer-by-layer methodology to form multilayers via vesicle rupture onto existing supported bilayers (SLBs) using poly l-lysine (PLL) an electrostatic polymer linker. The assembly process was monitored at the...

10.1021/acs.biomac.5b01434 article EN cc-by Biomacromolecules 2015-12-07

Site-directed mutagenesis and functionalization of gold surfaces have been combined to obtain a stable immobilization the heme domain cytochrome P450 BM3 from Bacillus megaterium. Immobilization experiments were carried out using wild type protein bearing surface C62 C156 site-directed mutants C62S, C156S, double mutant C62S/C156S (no exposed cysteines). The was functionalized two different spacers: cystamine-N-succinimidyl 3-maleimidopropionate dithio-bismaleimidoethane, both leading...

10.1021/ac8011413 article EN Analytical Chemistry 2008-10-24

[FeFe]-hydrogenases are efficient natural catalysts that can be exploited for hydrogen production. Immobilization of the recombinant [FeFe]-hydrogenase CaHydA was achieved first time on an anatase TiO2 electrode. The enzyme is able to interact and exchange electrons with electrode catalyze production efficiency 70%.

10.1039/c1cc14535e article EN Chemical Communications 2011-01-01

Oriented immobilization of human cytochrome P450 2E1 and its catalytic activity by direct electrochemistry was achieved engineering two multisite mutants 2E1: MUT261 (C268S−C480S−C488S) MUT268 (C261S−C480S−C488S). Here, all the exposed cysteines are mutated into serines, with exception one (C261 for C268 MUT268) that is able to link covalently a modified gold electrode. The wild type, as well mutants, were immobilized onto electrodes using dithio-bismaleimidoethane self-assembled monolayer....

10.1021/ac101072h article EN Analytical Chemistry 2010-05-27

This paper is the first report of a P450-electrode in microfluidic format. A 30 μL cell was made poly(methyl methacrylate) containing inlet, outlet, and reaction chamber with two electrode strips, one which contains human cytochrome P450 3A4 covalently bound to gold via 6-hexanethiol 7-mercaptoheptanoic acid (1:1) self-assembled monolayer. The electrochemical response tested using four drugs that are known substrates 3A4: quinidine, nifedipine, alosetron ondansetron. Titration experiments...

10.1021/ac102480k article EN Analytical Chemistry 2010-11-24

A gene coding for a class VII cytochrome P450 monooxygenase (CYP116B5) was identified from Acinetobacter radioresistens S13 growing on media with medium (C14, C16) and long (C24, C36) chain alkanes as the sole energy source. Phylogenetic analysis of its N- C-terminal domains suggests an evolutionary model involving plasmid-mediated horizontal transfer donor Rhodococcus jostii RHA1 to receiving A. S13. This event followed by fusion integration new in chromosome. Heterologous expression...

10.1111/mmi.12883 article EN Molecular Microbiology 2014-11-26

Human aromatase (CYP19A1) is a steroidogenic cytochrome P450 converting androgens into estrogens. No ligand-free crystal structure of the enzyme available to date. The in complex with substrate androstenedione and steroidal inhibitor exemestane shows very compact conformation enzyme, leaving unanswered questions on conformational changes that must occur allow access ligand active site. As H/D exchange kinetics followed by FTIR spectroscopy can provide information proteins where solvent...

10.1371/journal.pone.0082118 article EN cc-by PLoS ONE 2013-12-11

Human liver cytochrome P450 3A4 is the main enzyme involved in drug metabolism. This makes it an attractive target for biocatalytic applications, such as synthesis of pharmaceuticals and metabolites. However, its poor solubility, stability low coupling have limited application biotechnological context. We previously demonstrated that solubility can be increased by creating fusion proteins between reductase from Bacillus megaterium BM3 (BMR) N-terminally modified (3A4-BMR). In this work, we...

10.3389/fphar.2017.00121 article EN cc-by Frontiers in Pharmacology 2017-03-21
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