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Related Concept Videos

Drug Binding to Blood Components01:30

Drug Binding to Blood Components

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).
HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are further...
Drug Distribution: Tissue Binding01:21

Drug Distribution: Tissue Binding

Upon entering the systemic circulation, drugs can distribute into the interstitial and intracellular fluid of various tissue cells. This distribution is facilitated by the binding of drugs to different cellular components within tissues, which may lead to drug accumulation in specific areas. Drugs bound to tissue components serve as reservoirs that release free drugs back into the system, prolonging the drug's overall action. However, this accumulation can also result in local toxicity.
For...
Drug Distribution: Plasma Protein Binding01:29

Drug Distribution: Plasma Protein Binding

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...
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...
Physiological Pharmacokinetic Models: Assumption with Protein Binding01:13

Physiological Pharmacokinetic Models: Assumption with Protein Binding

Physiological models with protein binding in pharmacokinetics offer a sophisticated approach to understanding drug disposition. These models consider drug-protein interactions, enabling them to effectively predict drug concentrations in different organs and tissues. This precision aids in accurate drug dosing, providing a significant advantage over conventional models. A key process within these models is equilibration, which ensures that drug concentrations achieve a steady state within the...
Factors Affecting Protein-Drug Binding: Patient-Related Factors01:29

Factors Affecting Protein-Drug Binding: Patient-Related Factors

Protein-drug binding, a pivotal aspect of pharmacokinetics, is subject to considerable variability influenced by an array of patient-related factors. The intricate interplay of age, individual differences, and pathological conditions significantly impact the binding dynamics and subsequent pharmacological effects.
Age stands as a key determinant in protein-drug binding. Neonates, characterized by low albumin content, experience heightened concentrations of unbound drugs such as phenytoin and...

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Related Experiment Video

Updated: Jun 7, 2026

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
11:07

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

Published on: September 21, 2011

Corticosteroid-binding globulin regulates cortisol pharmacokinetics.

I Perogamvros1, L Aarons, A G Miller

  • 1Department of Endocrinology, Christie Hospital, Manchester Academic Health Science Centre, UK.

Clinical Endocrinology
|November 9, 2010
PubMed
Summary
This summary is machine-generated.

Corticosteroid-binding globulin (CBG) affects cortisol pharmacokinetics. While free cortisol remains stable in CBG null individuals, women on oral contraceptives may experience altered free cortisol levels, potentially leading to overexposure.

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Primary Culture of Rat Adrenocortical Cells and Assays of Steroidogenic Functions
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Primary Culture of Rat Adrenocortical Cells and Assays of Steroidogenic Functions
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Primary Culture of Rat Adrenocortical Cells and Assays of Steroidogenic Functions

Published on: March 12, 2019

Area of Science:

  • Endocrinology
  • Pharmacokinetics
  • Biochemistry

Background:

  • Corticosteroid-binding globulin (CBG) is the primary cortisol transporter in circulation.
  • Changes in CBG binding capacity are thought to influence total cortisol levels but not free cortisol.
  • The pharmacokinetics (PK) of unbound cortisol in relation to CBG variations remain understudied.

Purpose of the Study:

  • To investigate the impact of CBG on cortisol pharmacokinetics.
  • To assess how variations in CBG function affect the disposition of cortisol.

Main Methods:

  • Studied women on oral contraceptives (OCP), CBG null individuals, and healthy volunteers (HV).
  • Administered hydrocortisone intravenously and orally.
  • Analyzed pharmacokinetic parameters for total serum cortisol (SerF), free serum cortisol (FreeF), and salivary cortisol (SalF).

Main Results:

  • Following IV hydrocortisone, OCP users showed higher SerF AUC and half-life, while CBG null individuals had lower values compared to HV.
  • SerF clearance and volume of distribution were altered in OCP users and CBG null individuals.
  • FreeF and salivary cortisol PK parameters did not differ between CBG null and HV, but OCP users exhibited higher AUC and prolonged half-life for FreeF.

Conclusions:

  • CBG significantly influences cortisol pharmacokinetics.
  • Disrupted CBG binding maintains normal free cortisol PK, but CBG null individuals lack a readily releasable cortisol pool.
  • Women using oral contraceptives may have altered free cortisol kinetics, potentially leading to glucocorticoid overexposure.