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Related Concept Videos

Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

Factors Affecting Protein-Drug Binding: Protein-Related Factors

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Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
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Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
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When drugs enter systemic circulation, they interact with various components of the blood, including proteins such as human serum albumin (HSA), α1-acid glycoprotein (AAG), lipoproteins, globulins, and red blood cells (RBCs).
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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
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A Liquid Phase Affinity Capture Assay Using Magnetic Beads to Study Protein-Protein Interaction: The Poliovirus-Nanobody Example
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Aggregation Properties of Albumin in Interacting with Magnetic Fluids.

Elena N Velichko1, Elina K Nepomnyashchaya1, Maksim A Baranov1

  • 1Institute of Electronics and Telecommunications, Peter the Great St. Petersburg Polytechnic University, 195251 Saint Petersburg, Russia.

International Journal of Molecular Sciences
|October 13, 2021
PubMed
Summary

Interactions between iron oxide nanoparticles and albumin were studied. Low concentrations of nanoparticles enhanced albumin film stability, while high concentrations disrupted it, impacting biomolecular film applications.

Keywords:
dynamic light scatteringmagnetic fluidmolecular electronicsnanoparticle sizingprotein–nanoparticle interactionself-organization

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Physical Chemistry

Background:

  • Serum albumin is a crucial biomolecule with diverse applications.
  • Interactions between biomolecules and magnetic nanoparticles are vital for developing advanced materials.
  • Understanding these interactions is key to controlling the properties of biomolecular films.

Purpose of the Study:

  • To investigate the effects of iron(II,III) oxide (Fe3O4) magnetic nanoparticles on serum albumin in aqueous solutions.
  • To characterize the formation of aggregates and the stability of resulting biomolecular films.
  • To determine optimal concentrations of Fe3O4 nanoparticles for stable albumin-based films.

Main Methods:

  • Laser correlation spectroscopy was used to analyze particle sizes in solution.
  • Optical analysis of dehydrated films assessed structural morphology and stability.
  • Studies were conducted across a range of Fe3O4 nanoparticle concentrations.

Main Results:

  • Low Fe3O4 concentrations (up to 10^-6 g/L) formed small aggregates (up to 300 nm), enhancing albumin film stability and spiral structure formation.
  • High Fe3O4 concentrations (from 10^-4 g/L) led to large aggregates (>1000 nm), disrupting film morphology and decreasing stability.
  • Optimal stability was observed at Fe3O4 concentrations below 10^-4 g/L, correlating with small albumin-nanoparticle aggregates.

Conclusions:

  • The concentration of Fe3O4 magnetic nanoparticles significantly influences the aggregation behavior with albumin and the stability of biomolecular films.
  • Low concentrations promote stable structures, while high concentrations lead to instability.
  • These findings are crucial for predicting and controlling the stability of biomolecular films incorporating magnetic nanoparticles.