Publications by authors named "F Terki"

In the framework of a protein-ligand-fishing strategy to identify proteins that bind to trans-resveratrol, a natural phenolic compound with pharmacological benefits, we have developed magnetic nanoparticles covalently linked to trans-resveratrol through three different derivatives and examined their aggregation behavior in aqueous solution. The monodispersed magnetic core (18 nm diameter) with its mesoporous silica shell (93 nm diameter) exhibited a notable superparamagnetic behavior useful for magnetic bioseparation. The hydrodynamic diameter, deduced from dynamic light scattering analysis, of the nanoparticle increased from 100 to 800 nm when the aqueous buffer changed from pH 10.

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Electronic structures and thermoelectric (TE) properties of KBiBa and KBiSr half-Heusler compounds are investigated by using the combined framework of first-principles and semi-classical Boltzmann transport theory. Elastic and phonon properties calculations reveal that these compounds are mechanically and dynamically stable. Band structures calculations, using the Tran and Blaha modified Becke-Johnson potential including spin-orbit coupling, show that KBiBa and KBiSr compounds are semiconductors with an indirect bandgap of 0.

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The global burden of malnutrition remains unacceptably high. Malnutrition is a universal issue restricting development and slowing progress. Malnutrition is responsible for more illness and ill-health than any other cause worldwide.

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Article Synopsis
  • The study investigates the interaction between trans-resveratrol and the enzyme lipase (CpLIP2) using various analytical methods, revealing that tryptophan residues play a key role in fluorescence quenching.
  • A thermodynamic analysis indicates a single binding site for trans-resveratrol with a binding free energy of -24 kJ/mol, while also showing that it inhibits lipase activity competitively.
  • Molecular docking and quantum-chemical calculations demonstrate a strong binding affinity of trans-resveratrol to the catalytic site of CpLIP2, highlighting significant electrostatic and hydrophobic interactions that could aid in the screening of similar compounds.
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