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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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Factors Affecting Protein-Drug Binding: Drug-Related Factors01:18

Factors Affecting Protein-Drug Binding: Drug-Related Factors

60
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...
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Factors Affecting Protein-Drug Binding: Drug Interactions01:23

Factors Affecting Protein-Drug Binding: Drug Interactions

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Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
71
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Protein-Drug Binding: Mechanism and Kinetics01:16

Protein-Drug Binding: Mechanism and Kinetics

170
Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
170
Drug Distribution: Plasma Protein Binding01:29

Drug Distribution: Plasma Protein Binding

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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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Saturated Fatty Acids Induce Ceramide-associated Macrophage Cell Death
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Broad PFAS binding with fatty acid binding protein 4 is enabled by variable binding modes.

Aaron S Birchfield1, Faik N Musayev2,3, Abdul J Castillo1

  • 1Department of Chemistry, Virginia Commonwealth University, Richmond, VA 23284, U.S.A.

Biorxiv : the Preprint Server for Biology
|April 8, 2025
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Summary
This summary is machine-generated.

Human adipocyte fatty acid-binding protein (FABP4) binds various per- and polyfluoroalkyl substances (PFAS), including replacements for legacy chemicals. Structural analysis reveals distinct binding modes, impacting toxicological outcomes and metabolic regulation.

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Area of Science:

  • Environmental Chemistry
  • Structural Biology
  • Toxicology

Background:

  • Per- and polyfluoroalkyl substances (PFAS) are widespread environmental pollutants known to bioaccumulate.
  • The molecular mechanisms underlying PFAS interactions with biological proteins are not well understood.
  • Human adipocyte fatty acid-binding protein (FABP4) plays a role in metabolic regulation and endocrine function.

Purpose of the Study:

  • To investigate the binding interactions between FABP4 and a diverse range of PFAS.
  • To elucidate the structural basis of PFAS-FABP4 complex formation.
  • To understand how PFAS binding to FABP4 may influence metabolic processes and disease risk.

Main Methods:

  • Fluorescence competition assays to measure binding affinities.
  • X-ray crystallography to determine the structures of FABP4 in complex with specific PFAS (PFOA, PFDA, PFHxDA).
  • Analysis of binding modes and their correlation with chemical properties.

Main Results:

  • FABP4 binds a variety of PFAS, including newer replacements and longer-chain compounds.
  • Shorter-chain PFAS exhibit measurable binding affinities to FABP4, exceeding those of nonfluorinated analogs.
  • Crystal structures reveal three distinct binding modes for PFOA, PFDA, and PFHxDA, with PFOA binding in two sites.
  • Binding modes involve enhanced hydrophobic interactions and distinct protein conformations, explaining observed affinities.

Conclusions:

  • PFAS-FABP4 interactions are influenced by PFAS chain length, headgroup, and protein conformation.
  • PFAS binding to FABP4, even at low affinities, could perturb metabolic regulation due to FABP4's role in endocrine function.
  • Structural and biochemical insights are crucial for understanding PFAS transport and toxicological effects.