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Related Concept Videos

Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

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

Factors Affecting Protein-Drug Binding: Protein-Related Factors

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 bound by...
Factors Affecting Protein-Drug Binding: Drug-Related Factors01:18

Factors Affecting Protein-Drug Binding: Drug-Related Factors

Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In contrast,...

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Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
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Structural changes in apolipoproteins bound to nanoparticles.

Risto Cukalevski1, Martin Lundqvist, Cecilia Oslakovic

  • 1Biochemistry and Structural Biology, Lund University, Lund, Sweden. risto.cukalevski@biochemistry.lu.se

Langmuir : the ACS Journal of Surfaces and Colloids
|October 8, 2011
PubMed
Summary
This summary is machine-generated.

Nanoparticle surface charge significantly alters protein structure, impacting human health. Opposite charges cause major changes in proteins like apolipoprotein A-I and human serum albumin, while similar charges have less effect.

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Published on: May 13, 2020

Area of Science:

  • Biophysics
  • Materials Science
  • Biochemistry

Background:

  • Nanoparticles are prevalent in pharmaceuticals and food, raising concerns about human exposure.
  • The protein corona formed on nanoparticles influences their biological interactions, but structural effects are poorly understood.

Purpose of the Study:

  • To investigate how nanoparticle surface charge affects the structure of adsorbed proteins.
  • To determine if surface charge is a universal predictor of protein structural changes.

Main Methods:

  • Circular dichroism spectroscopy
  • Fluorescence spectroscopy
  • Limited proteolysis
  • Adsorption of apolipoprotein A-I, apolipoprotein B100, HDL, human serum albumin, and lysozyme onto polystyrene nanoparticles with varying surface charges.

Main Results:

  • Nanoparticle surface charge significantly impacts protein secondary and tertiary structures.
  • Oppositely charged nanoparticles induced greater structural changes in apolipoprotein A-I and human serum albumin compared to similarly charged ones.
  • Apolipoprotein B100 structure was perturbed by all tested nanoparticles.

Conclusions:

  • Nanoparticle surface charge is a critical factor influencing protein structure.
  • The specific protein and its net charge determine the extent of structural modification.
  • Understanding these interactions is crucial for assessing nanoparticle safety in biological systems.