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Related Concept Videos

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...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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,...
Protein-Drug Binding: Mechanism and Kinetics01:16

Protein-Drug Binding: Mechanism and Kinetics

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,...
Site-Targeted Drug Delivery Systems: Polymeric Carriers01:24

Site-Targeted Drug Delivery Systems: Polymeric Carriers

Polymeric carriers enhance targeted drug delivery by increasing efficacy while minimizing off-target effects. These carriers comprise a biodegradable polymeric backbone integrated with functional elements that enable targeting, improve physicochemical properties, and regulate drug release.Targeting MechanismsThe targeting ability of polymeric carriers is mediated by a homing device, which is a molecular recognition component designed to selectively bind to specific tissues or cells. Monoclonal...

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Functionality of proteins bound to plasma polymer surfaces.

Bryan R Coad1, Tanja Scholz, Krasimir Vasilev

  • 1Ian Wark Research Institute, University of South Australia, Mawson Lakes 5095 SA Australia. Bryan.Coad@unisa.edu.au

ACS Applied Materials & Interfaces
|April 12, 2012
PubMed
Summary

Plasma polymerization creates functional surfaces for bio-interfaces. Aldehyde-based surfaces enable specific streptavidin binding, preserving function, while ethanol-based surfaces lead to nonspecific adsorption and loss of biotin binding ability.

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Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Biophysics

Background:

  • Plasma polymerization allows surface functionalization for biointerfacial applications.
  • Understanding protein-surface interactions is crucial for biomaterial development.
  • Distinguishing specific vs. nonspecific protein binding and its impact on functionality is key.

Purpose of the Study:

  • To investigate protein binding mechanisms on plasma polymer surfaces.
  • To compare protein adsorption and functionality on propionaldehyde and ethanol plasma polymers.
  • To correlate plasma polymer structure with protein binding behavior.

Main Methods:

  • Deposition of plasma polymer (pp) films using propionaldehyde and ethanol at varying powers.
  • Surface characterization using X-ray photoelectron spectroscopy (XPS).
  • Assessment of streptavidin (SAV) and human serum albumin (HSA) adsorption and biotin binding functionality.

Main Results:

  • Propionaldehyde pp surfaces facilitated specific, functional streptavidin immobilization.
  • Ethanol pp surfaces showed reduced protein adsorption at low power (5 W), likely due to hydroxyl group retention and hydration.
  • Streptavidin adsorbed to ethanol pp surfaces lost its biotin binding ability, suggesting denaturation via nonspecific adsorption.

Conclusions:

  • Surface chemistry dictates protein binding mechanisms and retained functionality.
  • Aldehyde groups promote specific protein chemisorption, preserving biological activity.
  • Nonspecific adsorption on ethanol pp surfaces leads to protein denaturation, irrespective of surface hydrophilicity.