Interaction between the Antimalarial Drug Dispiro-Tetraoxanes and Human Serum Albumin: A Combined Study with Spectroscopic Methods and Computational Studies
Priyanka Yadav, Bhawana Sharma, Chiranjeev Sharma, Preeti Singh, Satish Kumar Awasthi
Abstract
) indicated the moderate affinity of the analogues to HSA. CD confirmed the conformational changes in the serum albumin upon interaction with these analogues. Molecular docking validated the empirical results as these two analogues bind through hydrophobic interactions and hydrogen bonding with HSA. Present work first defined the binding mechanism of dispiro-tetraoxanes with HSA and thus provides a fresh insight into the drug transportation and metabolism. The present study could direct toward designing more potent tetraoxane analogues for their use in the biomedical field.
Topics & Concepts
Human serum albuminChemistryCircular dichroismHydrogen bondDocking (animal)Quenching (fluorescence)Plasmodium falciparumHydrophobic effectFluorescenceDrugAlbuminCombinatorial chemistryBinding siteSerum albuminStereochemistryBiochemistryMoleculePharmacologyOrganic chemistryMalariaBiologyMedicineQuantum mechanicsNursingImmunologyPhysicsProtein Interaction Studies and Fluorescence AnalysisDrug Transport and Resistance MechanismsSurfactants and Colloidal Systems