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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...
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...

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Related Experiment Video

Updated: Jun 22, 2026

Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method
09:43

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Published on: April 11, 2020

Human plasma protein adsorption on carbon-based materials.

Michele Vinante1, Gabriella Digregorio, Lorenzo Lunelli

  • 1FBK-irst, Via Sommarive 18, 38050 Povo, TN, Italy.

Journal of Nanoscience and Nanotechnology
|June 10, 2009
PubMed
Summary

Different carbon materials react uniquely with blood plasma proteins. Pyrolytic carbon shows low protein and Hageman factor adsorption but high fibrinogen adhesion, unlike other materials studied.

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Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Hematology

Background:

  • Protein adsorption and conformational changes on material surfaces are critical for biological interactions.
  • Understanding these interactions is key for developing biocompatible materials, especially for blood-contacting applications.

Purpose of the Study:

  • To investigate the initial interactions of various carbon-based materials with human blood plasma.
  • To compare protein adsorption patterns on multi-walled carbon nanotubes (MWCNTs), highly oriented pyrolytic graphite (HOPG), nanocrystalline graphite (NG), and pyrolytic carbon (PyC).

Main Methods:

  • Exposure of materials to platelet-poor plasma (PPP) followed by protein quantification using Micro BCA Protein Assay.
  • Immunofluorescence analysis to detect fibrinogen (Fg) and Hageman factor (FXII) surface density and distribution.
  • Surface characterization using X-ray photoelectron spectroscopy (XPS), scanning electron microscopy (SEM), and atomic force microscopy (AFM).

Main Results:

  • Pyrolytic carbon (PyC) exhibited low whole protein and FXII adsorption but high Fg adsorption.
  • MWCNTs, NG, and HOPG showed progressively higher whole protein adsorption compared to PyC.
  • Fg adsorption was high on PyC, NG, and MWCNTs, while FXII was only detected on HOPG.

Conclusions:

  • Surface chemistry, particularly revealed by XPS, significantly influences protein adsorption, more so than surface morphology (AFM).
  • PyC demonstrates distinct protein adsorption properties compared to MWCNTs, NG, and HOPG, suggesting potential for specific anti-thrombogenic applications.
  • The study highlights the differential adsorption of key proteins like Fg and FXII on carbon materials, impacting their biocompatibility.