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Related Concept Videos

Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

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Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
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Raman Spectroscopy: Overview01:20

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The underlying principle of Raman spectroscopy is based on the interaction between light and matter, specifically molecules' inelastic scattering of photons. When a monochromatic beam of light, typically from a laser source, interacts with a sample, most scattered light has the same frequency as the incident light. This is known as Rayleigh scattering.
However, a small fraction of the scattered light exhibits a frequency shift due to the exchange of energy between the incident photons and...
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Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions
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Analysis of Biologics Molecular Descriptors towards Predictive Modelling for Protein Drug Development Using

Jaakko Itkonen1, Leo Ghemtio1, Daniela Pellegrino1

  • 1Drug Research Program, Division of Pharmaceutical Biosciences, Faculty of Pharmacy, University of Helsinki, 00100 Helsinki, Finland.

Pharmaceutics
|August 26, 2022
PubMed
Summary
This summary is machine-generated.

Time-gated Raman spectroscopy monitors pharmaceutical protein unfolding in real-time. This method enables inline analysis, correlating unfolding events with traditional techniques for predictive modeling.

Keywords:
CDDLSK-means clusteringPCARaman spectroscopybiologicsin-line measurementpharmaceutical proteinsprotein unfoldingtryptophan fluorescence

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Area of Science:

  • Biophysical Chemistry
  • Pharmaceutical Analysis
  • Spectroscopy

Background:

  • Pharmaceutical proteins are fragile and prone to unfolding and aggregation.
  • Current analytical methods for protein monitoring are often offline and cannot assess real-time folding dynamics.
  • Orthogonal analytical techniques are crucial for production and market surveillance of biologics.

Purpose of the Study:

  • To introduce time-gated Raman spectroscopy for monitoring protein unfolding.
  • To identify molecular descriptors indicative of protein unfolding.
  • To establish a foundation for predictive modeling of protein unfolding events.

Main Methods:

  • Utilized time-gated Raman spectroscopy for label-free, in-line, real-time protein unfolding analysis.
  • Employed K-means clustering and Principal Component Analysis (PCA) for data interpretation.
  • Correlated spectroscopic data with traditional analytical methods.

Main Results:

  • Demonstrated the capability of time-gated Raman spectroscopy to detect protein unfolding.
  • Successfully correlated local unfolding events with established analytical techniques.
  • Established Raman spectroscopy as a viable tool for in-line monitoring of protein stability.

Conclusions:

  • Time-gated Raman spectroscopy offers a powerful, real-time, label-free approach for monitoring pharmaceutical protein unfolding.
  • This technique facilitates inline process analytical technology (PAT) for biologics.
  • The study represents a significant advancement towards predictive modeling of protein stability during manufacturing and storage.