The ligand-protein interaction plays a central role in the regulation of biological processes, like cellular metabolism and signal transmission. The term ligand encompasses nucleic acids, cofactors, metals, other proteins, and drugs. Protein activity can be affected by its interaction with specific ligands through different mechanisms. The analysis of protein-ligand interaction is crucial to understand the regulation of biological function, elucidate how a pathology is triggered, and discover new bioactive compounds capable to modulate the protein function.
The identification and characterization of protein-ligand interaction are central in the drug discovery program because they enable the rapid identification of potential drugs, as well as contributes to advancement from hits to leads. In this context, several analytical techniques have emerged as a useful tool to develop new, rapid, and reliable screening assays.
The target-based drug discovery program is greatly dependent on the development of high-throughput and reliable analytical methods to monitor protein-ligand interactions. Diverse analytical techniques are available to identify and characterize protein ligand-interaction, including the MS-based approaches, surface plasmon resonance (SPR), nuclear magnetic resonance (NMR), LC-based assays, quartz crystal microbalance, light-scattering, circular dichroism.
This collection focuses on the protagonism of the different analytical methods in the early stages of new drugs development to evidence the applicability and usefulness of those tools to monitor and characterize ligand-protein interactions. We hope this special issue would be helpful for the researchers from academia and pharmaceutical industries focused on innovative analytical methods to accelerate the drug discovery program.
This Research Topic invites contributions, such as Original Research articles, Reviews, and Mini-Reviews on the recent advances in the analytical methods to monitor ligand-protein interaction in screening assays. Potential topics include, but are not limited to:
- NMR binding experiments for the characterization of ligand-protein interaction (including transferred nuclear Overhauser effect, saturation transfer difference spectroscopy, and water–ligand interactions observed via gradient spectroscopy experiments)
- MS-based assays for ligand screening (like in solution methods: hydrogen/deuterium exchange of protein backbone amide hydrogens and photoaffinity labeling, as well as analysis of intact noncovalent protein-ligand complexes
- Ligand fishing assays
- LC-based screening assays (activity or affinity-based; online or offline)
- Surface plasmon resonance for ligand-protein binding studies
- Quartz crystal microbalance in ligand screening assays
- Light-scattering, circular dichroism, and other analytical techniques employed in the development of innovative screening assays
-Capillary electrophoresis approaches.
The ligand-protein interaction plays a central role in the regulation of biological processes, like cellular metabolism and signal transmission. The term ligand encompasses nucleic acids, cofactors, metals, other proteins, and drugs. Protein activity can be affected by its interaction with specific ligands through different mechanisms. The analysis of protein-ligand interaction is crucial to understand the regulation of biological function, elucidate how a pathology is triggered, and discover new bioactive compounds capable to modulate the protein function.
The identification and characterization of protein-ligand interaction are central in the drug discovery program because they enable the rapid identification of potential drugs, as well as contributes to advancement from hits to leads. In this context, several analytical techniques have emerged as a useful tool to develop new, rapid, and reliable screening assays.
The target-based drug discovery program is greatly dependent on the development of high-throughput and reliable analytical methods to monitor protein-ligand interactions. Diverse analytical techniques are available to identify and characterize protein ligand-interaction, including the MS-based approaches, surface plasmon resonance (SPR), nuclear magnetic resonance (NMR), LC-based assays, quartz crystal microbalance, light-scattering, circular dichroism.
This collection focuses on the protagonism of the different analytical methods in the early stages of new drugs development to evidence the applicability and usefulness of those tools to monitor and characterize ligand-protein interactions. We hope this special issue would be helpful for the researchers from academia and pharmaceutical industries focused on innovative analytical methods to accelerate the drug discovery program.
This Research Topic invites contributions, such as Original Research articles, Reviews, and Mini-Reviews on the recent advances in the analytical methods to monitor ligand-protein interaction in screening assays. Potential topics include, but are not limited to:
- NMR binding experiments for the characterization of ligand-protein interaction (including transferred nuclear Overhauser effect, saturation transfer difference spectroscopy, and water–ligand interactions observed via gradient spectroscopy experiments)
- MS-based assays for ligand screening (like in solution methods: hydrogen/deuterium exchange of protein backbone amide hydrogens and photoaffinity labeling, as well as analysis of intact noncovalent protein-ligand complexes
- Ligand fishing assays
- LC-based screening assays (activity or affinity-based; online or offline)
- Surface plasmon resonance for ligand-protein binding studies
- Quartz crystal microbalance in ligand screening assays
- Light-scattering, circular dichroism, and other analytical techniques employed in the development of innovative screening assays
-Capillary electrophoresis approaches.