The immobilization of macromolecules on chromatographic supports, or biochromatography, has been proposed in 1969 by Soczewinsky and Bieganowska. The idea to model a biological event into an in-flow analytical system finds its rationale on the scientific evidence that the same interactions occurring in a biological environment can be reproduced in a chromatographic system. Since then, immobilized enzymes, proteins and receptors have been used to study kinetic mechanisms or characterize ligand-receptor binding interactions in medicinal chemistry programs.
The present project is aimed at collecting the most recent and innovative applications of analytical systems based on immobilized macromolecules (i.e. proteins, peptides, enzymes), applied to the study of structure and affinity/activity of molecules, or used to optimize either small or high molecular weight molecules of pharmaceutical interest.
In the last years, the recent advances in materials technology and instrumentation, lead to the development of new supports, devices and innovative analytical platforms for the preparation and optimization of molecules of pharmaceutical interest.
This research topic will be a reference for authors pushing analytical technologies towards advanced applications in medicinal chemistry.
In this Research Topic, we will collect innovative and original research papers describing the development and application of bioanalytical platforms including, but not limited to, the following topics:
• Emerging trends in biomaterials used for the immobilization of macromolecules for pharmaceutical applications.
• Development of analytical platforms and biochromatographic systems for drug / target interaction studies.
• Development and application of immobilized catalysts in innovative in-flow reaction systems for drug discovery applications.
• Application of immobilized catalysts for therapeutic proteins structural characterization.
• In flow modulation of therapeutic protein structural characteristics (i.e. glycosylation, glycan remodeling).
The immobilization of macromolecules on chromatographic supports, or biochromatography, has been proposed in 1969 by Soczewinsky and Bieganowska. The idea to model a biological event into an in-flow analytical system finds its rationale on the scientific evidence that the same interactions occurring in a biological environment can be reproduced in a chromatographic system. Since then, immobilized enzymes, proteins and receptors have been used to study kinetic mechanisms or characterize ligand-receptor binding interactions in medicinal chemistry programs.
The present project is aimed at collecting the most recent and innovative applications of analytical systems based on immobilized macromolecules (i.e. proteins, peptides, enzymes), applied to the study of structure and affinity/activity of molecules, or used to optimize either small or high molecular weight molecules of pharmaceutical interest.
In the last years, the recent advances in materials technology and instrumentation, lead to the development of new supports, devices and innovative analytical platforms for the preparation and optimization of molecules of pharmaceutical interest.
This research topic will be a reference for authors pushing analytical technologies towards advanced applications in medicinal chemistry.
In this Research Topic, we will collect innovative and original research papers describing the development and application of bioanalytical platforms including, but not limited to, the following topics:
• Emerging trends in biomaterials used for the immobilization of macromolecules for pharmaceutical applications.
• Development of analytical platforms and biochromatographic systems for drug / target interaction studies.
• Development and application of immobilized catalysts in innovative in-flow reaction systems for drug discovery applications.
• Application of immobilized catalysts for therapeutic proteins structural characterization.
• In flow modulation of therapeutic protein structural characteristics (i.e. glycosylation, glycan remodeling).
