Exploring the combination characteristics of lumefantrine, an antimalarial drug and human serum albumin through spectroscopic and molecular docking studies

Musa, Kabiru Abubakar; Ridzwan, Nor Farrah Wahidah; Mohamad, Saharuddin Bin; Tayyab, Saad

doi:10.1080/07391102.2020.1713215

Cited by 14 publications

(7 citation statements)

References 69 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Computer-aided drug design (CADD) approaches have been widely used to discover, develop, and analyze drugs and similar potential bioactive molecules, reducing time and cost. , These approaches are divided into ligand-based and structure-based drug designs. − The concept of structure-based drug design (SBDD) furnishes a deeper perceptive of the structure of the protein binding sites and various interlinkages coupled with them. − The principle of docking is based on an energy-based scoring relation that distinguishes the most fitted conformation of ligand when accommodated to the receptor binding pocket. − The extensive approach is based on the fact that lower energy scores suggest for more suitable binding of receptors and ligands in comparison to greater values of energy scores. In this way, the molecular docking aims at achieving a suitable ligand binding mode with the smallest energy .…”

Section: Introductionmentioning

confidence: 99%

Predictions of Drug–Protein Interactions and Study of Magnetically Assisted Release Dynamics of 5-Fluorouracil from Soya Protein-Coated Iron Oxide Core–Shell Nanoparticles

Jain¹,

Sonker²,

Bajpai³

et al. 2020

ACS Appl. Bio Mater.

View full text Add to dashboard Cite

In silico studies were performed using 5-fluorouracil (5-FU) to explore the efficacy of template docking and facilitate designing of drug nanocarrier systems. The binding of human uridine phosphorylase (huPP1) with 5-FU was found to show the following interactions: (1) hydrogen bonds were alleviated by a network of GLN217 and ARG219, (2) hydrophobic interactions were shown by PHE213, THR141, LEU272, and ILE281 (3) positive electrostatic interactions were shown by PHE213, THR141, LEU272, SER142, GLU248, and GLY143. As an experimental supplementation and validation to the adopted computational approach, 5- FU-loaded soya protein-coated iron oxide (SPCIO) core–shell nanoparticles were prepared following microemulsion and co-precipitation techniques and subsequently characterized by FTIR, particle size and zeta potential studies, TEM, XRD, and DSC techniques. Whereas the FTIR spectra confirm the presence of the soya protein and drug 5-FU in the nanoparticles, the zeta potential was found to be suppressed due to the loading of 5-FU. The XRD study confirmed the crystalline nature of the drug-loaded nanoparticles. TEM analysis suggested that the nanoparticles have sizes up to 200 nm and the morphology and size remain almost the same even after loading of the drug 5-FU onto nanoparticles. The soya protein-coated iron oxide nanoparticles demonstrated zero cytotoxicity against fibroblast cells. The controlled release of 5-FU was studied in vitro, and the effects of pH, chemical composition of nanoparticles, extent of drug loading, and simulated biofluids on the controlled release of 5-FU were studied. The swelling of nanoparticles and release of 5-FU were found to increase with increasing strength of the externally applied magnetic field.

show abstract

Section: Introductionmentioning

confidence: 99%

Predictions of Drug–Protein Interactions and Study of Magnetically Assisted Release Dynamics of 5-Fluorouracil from Soya Protein-Coated Iron Oxide Core–Shell Nanoparticles

Jain¹,

Sonker²,

Bajpai³

et al. 2020

ACS Appl. Bio Mater.

View full text Add to dashboard Cite

show abstract

“…In a similar study by the same group, Lumefantrine was found to have a preferred binding site to HSA in Site I [102]. Furthermore, there were more hydrogen bonding interactions (one with Cys448) and a greater hydrophobic effect when the drug binds to Site I [102]. These were also observed in the binding characterization of Mefloquine with HSA [101].…”

Section: Interaction Of Antimalarial Drugs With Serum Albuminmentioning

confidence: 60%

“…Ano drug, Lumefantrine (Figure 14), is used in combination with other antimalarial drug treat malaria. In a similar study by the same group, Lumefantrine was found to ha preferred binding site to HSA in Site I [102]. Furthermore, there were more hydro…”

Section: Interaction Of Antimalarial Drugs With Serum Albuminmentioning

confidence: 65%

“…Another drug, Lumefantrine (Figure 14), is used in combination with other antimalarial drugs to treat malaria. In a similar study by the same group, Lumefantrine was found to have a preferred binding site to HSA in Site I [102]. Furthermore, there were more hydrogen bonding interactions (one with Cys448) and a greater hydrophobic effect when the drug Mefloquine (Figure 14) is an FDA-approved anti-malarial quinine derivative drug that attacks Plasmodium during the blood-stage of the parasite's life cycle [30][31][32].…”

Section: Interaction Of Antimalarial Drugs With Serum Albuminmentioning

confidence: 88%

See 1 more Smart Citation

Roles of Virtual Screening and Molecular Dynamics Simulations in Discovering and Understanding Antimalarial Drugs

Duay,

Yap,

Gaitano

et al. 2023

IJMS

View full text Add to dashboard Cite

Malaria continues to be a global health threat, with approximately 247 million cases worldwide. Despite therapeutic interventions being available, patient compliance is a problem due to the length of treatment. Moreover, drug-resistant strains have emerged over the years, necessitating urgent identification of novel and more potent treatments. Given that traditional drug discovery often requires a great deal of time and resources, most drug discovery efforts now use computational methods. In silico techniques such as quantitative structure-activity relationship (QSAR), docking, and molecular dynamics (MD) can be used to study protein-ligand interactions and determine the potency and safety profile of a set of candidate compounds to help prioritize those tested using assays and animal models. This paper provides an overview of antimalarial drug discovery and the application of computational methods in identifying candidate inhibitors and elucidating their potential mechanisms of action. We conclude with the continued challenges and future perspectives in the field of antimalarial drug discovery.

show abstract

“…Calorimetry is a powerful tool for detecting the perturbations on the protein unfolding process caused by an external agent, e.g., polymers or drugs [24][25][26][27]. UV-Vis titrations and, in general, spectroscopic studies (absorbance and fluorescence) are approaches that may appear simple but are, instead, tricky and powerful procedures that give interesting information on the binding mechanism [28,29]. Mass spectrometry gave additional value to the study and enabled to define the molecular identity of the adduct formed with the binding.…”

Section: Introductionmentioning

confidence: 99%

Thermodynamic Evaluation of the Interactions between Anticancer Pt(II) Complexes and Model Proteins

et al. 2021

View full text Add to dashboard Cite

In this work, we have analysed the binding of the Pt(II) complexes ([PtCl(4′-phenyl-2,2′:6′,2″-terpyridine)](CF3SO3) (1), [PtI(4′-phenyl-2,2′:6′,2″-terpyridine)](CF3SO3) (2) and [PtCl(1,3-di(2-pyridyl)benzene) (3)] with selected model proteins (hen egg-white lysozyme, HEWL, and ribonuclease A, RNase A). Platinum coordination compounds are intensively studied to develop improved anticancer agents. In this regard, a critical issue is the possible role of Pt-protein interactions in their mechanisms of action. Multiple techniques such as differential scanning calorimetry (DSC), electrospray ionization mass spectrometry (ESI-MS) and UV-Vis absorbance titrations were used to enlighten the details of the binding to the different biosubstrates. On the one hand, it may be concluded that the affinity of 3 for the proteins is low. On the other hand, 1 and 2 strongly bind them, but with major binding mode differences when switching from HEWL to RNase A. Both 1 and 2 bind to HEWL with a non-specific (DSC) and non-covalent (ESI-MS) binding mode, dominated by a 1:1 binding stoichiometry (UV-Vis). ESI-MS data indicate a protein-driven chloride loss that does not convert into a covalent bond, likely due to the unfavourable complexes’ geometries and steric hindrance. This result, together with the significant changes of the absorbance profiles of the complex upon interaction, suggest an electrostatic binding mode supported by some stacking interaction of the aromatic ligand. Very differently, in the case of RNase A, slow formation of covalent adducts occurs (DSC, ESI-MS). The reactivity is higher for the iodo-compound 2, in agreement with iodine lability higher than chlorine.

show abstract

Exploring the combination characteristics of lumefantrine, an antimalarial drug and human serum albumin through spectroscopic and molecular docking studies

Cited by 14 publications

References 69 publications

Predictions of Drug–Protein Interactions and Study of Magnetically Assisted Release Dynamics of 5-Fluorouracil from Soya Protein-Coated Iron Oxide Core–Shell Nanoparticles

Predictions of Drug–Protein Interactions and Study of Magnetically Assisted Release Dynamics of 5-Fluorouracil from Soya Protein-Coated Iron Oxide Core–Shell Nanoparticles

Roles of Virtual Screening and Molecular Dynamics Simulations in Discovering and Understanding Antimalarial Drugs

Thermodynamic Evaluation of the Interactions between Anticancer Pt(II) Complexes and Model Proteins

Contact Info

Product

Resources

About