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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...
Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
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.
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Factors Affecting Protein-Drug Binding: Patient-Related Factors01:29

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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...
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
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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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Related Experiment Video

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Biochemical Reconstitution of Steroid Receptor&#x2022;Hsp90 Protein Complexes and Reactivation of Ligand Binding
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Corticosteroid-binding globulin: structure-function implications from species differences.

Bernd R Gardill1, Michael R Vogl, Hai-Yan Lin

  • 1Department of Biology, Lehrstuhl für Biotechnik, Friedrich-Alexander-University Erlangen-Nuremberg, Erlangen, Germany.

Plos One
|January 10, 2013
PubMed
Summary
This summary is machine-generated.

Corticosteroid-binding globulin (CBG) structure was analyzed, revealing a novel cleavage site in human CBG and explaining its lower progesterone affinity. Rat CBG

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Published on: July 5, 2018

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Endocrinology

Background:

  • Corticosteroid-binding globulin (CBG) is a key transporter of glucocorticoids and progesterone.
  • CBG belongs to the serine protease inhibitor (SERPIN) family, featuring a reactive center loop (RCL).
  • Proteolytic cleavage of the RCL typically induces a conformational change (stressed-to-relaxed transition) in SERPINs, affecting hormone binding.

Purpose of the Study:

  • To investigate the structure-function relationships of corticosteroid-binding globulin (CBG).
  • To characterize the conformational states of rat and human CBG.
  • To elucidate the molecular basis for progesterone binding affinity to CBG.

Main Methods:

  • X-ray crystallography (2.5 Å resolution) of human CBG complexed with progesterone.
  • Proteolytic cleavage assays.
  • Circular dichroism (CD) spectroscopy.
  • Thermal unfolding experiments.

Main Results:

  • A novel RCL cleavage site was identified in human CBG, distinct from known sites.
  • The cleaved RCL in human CBG integrates into β-sheet A, consistent with a stressed-to-relaxed transition.
  • Atomic interactions reveal lower binding affinity for progesterone compared to corticosteroids.
  • Rat CBG did not undergo the stressed-to-relaxed transition upon RCL cleavage, suggesting species-specific mechanisms.

Conclusions:

  • The structural mechanism of human CBG involves a novel RCL cleavage and subsequent S-to-R transition.
  • Species-specific differences exist in CBG's response to proteolytic cleavage.
  • The stressed-to-relaxed transition is not universally required for CBG function across species.