Search results for "BINDING INTERACTION"

showing 2 items of 2 documents

Nanoassemblies Based on Supramolecular Complexes of Nonionic Amphiphilic Cyclodextrin and Sorafenib as Effective Weapons to Kill Human HCC Cells

2015

Sorafenib (Sor), an effective chemiotherapeutic drug utilized against hepatocellular carcinoma (HOC), robustly interacts with nonionic amphiphilic cyclodextrin (aCD, SC6OH), forming, in aqueous solution, supramolecular complexes that behave as building blocks of highly water-dispersible colloidal nanoassemblies. SC6OH/Sor complex has been characterized by complementary spectroscopic techniques, such as UV-vis, steady-state fluorescence and anisotropy, resonance light scattering and H-1 NMR. The spectroscopic evidences and experiments carried out in the presence of an adamantane derivative, which competes with drug for CD cavity, agree with the entrapment of Sor in aCD, pointing out the role…

NiacinamideErythrocytesPolymers and PlasticsCell SurvivalAdamantaneDrug CompoundingSupramolecular chemistryBioengineeringNanotechnologyAdamantaneAntineoplastic AgentsBinding CompetitiveHemolysisAmphiphilic Cyclodextrins; Nanoparticles; Sorafenib; HCC cellsHCC cellsBiomaterialschemistry.chemical_compoundSurface-Active AgentsIn vivoCell Line TumorAmphiphileMaterials ChemistryHumanschemistry.chemical_classificationCyclodextrinsAqueous solutionCyclodextrinPhenylurea CompoundsSorafenibFluorescenceCombinatorial chemistrydigestive system diseasesNanostructuresBINDING INTERACTION THERAPY PHARMACOKINETICS BIOAVAILABILITY NANOPARTICLESDrug LiberationKineticsnanoassembliecyclodextrinchemistryDelayed-Action PreparationsProton NMRHepatocytes
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Thermodynamic analysis of the interactions between human ACE2 and spike RBD of Betacoronaviruses (SARS-CoV-1 and SARS-CoV-2)

2023

There are many scientific reports on the interaction of the SARS-CoV-2 virus S protein (and its RBD) with the human ACE2 receptor protein. However, there are no reliable data on how this interaction differs from the interaction of the receptor binding domain of SARS-CoV-1 with ACE2, in terms of binding strength and changes in reaction enthalpy and entropy. Our studies have revealed these differences and the impact of zinc ions on this interaction. Intriguingly, the binding affinity of both RBDs (of SARS-CoV-1 and of SARS-CoV-2) to the ACE2 receptor protein is almost identical; however, there are some differences in the entropic and enthalpic contributions to these interactions.

binding interactions; human ACE2; isothermal titration alorimetry; receptorbinding domain; SARS-CoV-1; SARS-CoV-2FEBS Open Bio
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