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Spectroscopic, Thermodynamic and Molecular Docking Studies on Molecular Mechanisms of Drug Binding to Proteins
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This reprint contains several articles where the molecular mechanisms and structural changes in target proteins on interaction with various viruses and bacteria were studied. In addition, drug-protein interactions, drug–drug interaction mechanisms, anti-Glycating, antioxidant, binding affinity, network pharmacology-driven investigations, and targeted anticancer treatments were also investigated.
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Keywords
- A. aspera
- advanced glycation end-products
- Ages
- Angiogenesis
- anti-glycation
- antidepressant
- antioxidant
- antipsychotics
- binding interaction
- bovine serum albumin
- C. gigantea
- C. procera
- caffeic acid
- Cancer
- CCL4
- charge transfer
- Competition
- coronary artery disease
- coumaric acid
- deep learning
- DFT
- DFTs
- Drug Design
- drug repurposing
- drug–protein interactions
- dynamics molecular docking
- ectodomain G protein
- enzyme assay
- erlotinib
- fluorescence quenching
- Fluorescence spectroscopy
- Garlic
- GC-MS
- glycation
- haloperidol
- Heparan sulfate
- Hepatitis E virus
- HSA
- human serum albumin
- Huperzine A
- hydrophobic interaction
- keratoconus
- MD simulations
- medicine
- methyltransferase
- Minimum inhibitory concentration (MIC)
- MM-GBSA calculations
- MMP-2
- MMP-9
- molecular docking
- molecular dynamic simulation
- Molecular Dynamics
- molecular dynamics simulation
- n/a
- NEK7
- network pharmacology
- Neurodegenerative disorders
- Neurotoxicity
- Other branches of medicine
- oxidative stress markers
- Pharmacology
- pharmacophore mapping
- Phytotherapy
- protein stability
- protein–ligand interaction
- quercetin
- quetiapine
- RSV
- seproxetine
- structural-based
- thermodynamic parameters
- Tuberculosis (TB)
- virtual screening
- VirtualToxLab
- Zebrafish
- α-amylase
- β-amyrin
- π-acceptors
Links
DOI: 10.3390/books978-3-0365-6225-4Editions