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Related Concept Videos

Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

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Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
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Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

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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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The Equilibrium Binding Constant and Binding Strength02:18

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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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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Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Estimating Virus Production Rates in Aquatic Systems
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Method for estimating protein binding capacity of polymeric systems.

Vaibhav Sharma1,2, Keith A Blackwood1,3, David Haddow4

  • 1RAFT Institute of Plastic Surgery, Mount Vernon Hospital, Northwood, HA6 2RN, UK.

Biochimie Open
|April 11, 2018
PubMed
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A new, cost-effective immuno-assay simplifies measuring protein adsorption on synthetic polymers. This method aids in developing advanced biomaterials for tissue engineering and other applications involving protein-surface interactions.

Keywords:
FibrinogenInterfacial bindingPolymeric surfacesProtein adsorption

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Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Tissue Engineering

Background:

  • Protein adsorption onto synthetic polymers is critical for composite biomaterial fabrication in tissue engineering.
  • Current methods for characterizing protein-polymer interfacial binding lack cost-effectiveness and simplicity.
  • Understanding protein-surface interactions is vital for designing functional biomaterials.

Purpose of the Study:

  • To introduce a simple, cost-effective, and robust three-step method for characterizing protein-polymer interfacial binding.
  • To evaluate the binding strength of fibrinogen on various synthetic polymer surfaces.
  • To assess the impact of protein-surface interaction strength on cell behavior.

Main Methods:

  • Synthetic polymer surface characterization (chemistry and roughness).
  • A novel immuno-based assay using protein extraction compounds to quantify protein binding strength.
  • In vitro 2D cell culture model to validate assay results.

Main Results:

  • Characterization revealed distinct surface chemistry and roughness for silicone, poly(acrylic acid)-coated silicone, and poly(allylamine)-coated silicone.
  • The novel immuno-based assay demonstrated significantly stronger fibrinogen binding to poly(acrylic acid) and poly(allylamine) coated silicone surfaces.
  • Cell studies confirmed that the protein-polymer interaction strength influenced cell growth.

Conclusions:

  • The developed immuno-based assay is a valuable tool for characterizing protein adsorption on synthetic polymers.
  • This method facilitates the development of advanced synthetic and protein-based composite biomaterials.
  • The findings have potential applications in fields where protein adsorption is a key factor.