Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Drug Binding to Blood Components

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: Plasma Protein Binding

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

DNA acidification by citric acid and gallic acid: acid binding site and DNA structural dynamics.

Journal of biomolecular structure & dynamics·2020

Same author

Locating the binding sites of citric acid and gallic acid on milk <i>β</i>-lactoglobulin.

Journal of biomolecular structure & dynamics·2020

Same author

Binding efficacy of aminobenzoic acid derivatives with DNA duplex: drug binding sites and DNA structure and dynamics.

Journal of biomolecular structure & dynamics·2020

Same author

Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis.

Journal of biomolecular structure & dynamics·2020

Same author

Application and biomolecular study of functionalized folic acid-dendrimer nanoparticles in drug delivery.

Journal of biomolecular structure & dynamics·2020

Same author

Complexation of cis-Pt and trans-Pt(NH<sub>3</sub>)<sub>2</sub>Cl<sub>2</sub> with serum proteins: A potential application for drug delivery.

Journal of biomolecular structure & dynamics·2019

Search research articles

Related Experiment Video

Updated: Jun 23, 2026

Dendrimer-based Uneven Nanopatterns to Locally Control Surface Adhesiveness: A Method to Direct Chondrogenic Differentiation

Dendrimer-based Uneven Nanopatterns to Locally Control Surface Adhesiveness: A Method to Direct Chondrogenic Differentiation

Published on: January 20, 2018

Dendrimers bind human serum albumin.

E Froehlich¹, J S Mandeville, C J Jennings

¹Département de Chimie-Biologie, Université du Quebec à Trois-Rivières, C. P. 500, Trois-Rivières, Québec, G9A 5H7, Canada.

The Journal of Physical Chemistry. B

|April 23, 2009

Summary

This study reveals how dendrimers interact with human serum albumin (HSA), a key drug transporter. Findings show dendrimers bind to HSA, altering its structure and suggesting potential impacts on drug delivery systems.

More Related Videos

Preparation and In Vitro Characterization of Dendrimer-based Contrast Agents for Magnetic Resonance Imaging

Preparation and In Vitro Characterization of Dendrimer-based Contrast Agents for Magnetic Resonance Imaging

Published on: December 4, 2016

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Related Experiment Videos

Last Updated: Jun 23, 2026

Dendrimer-based Uneven Nanopatterns to Locally Control Surface Adhesiveness: A Method to Direct Chondrogenic Differentiation

Dendrimer-based Uneven Nanopatterns to Locally Control Surface Adhesiveness: A Method to Direct Chondrogenic Differentiation

Published on: January 20, 2018

Preparation and In Vitro Characterization of Dendrimer-based Contrast Agents for Magnetic Resonance Imaging

Preparation and In Vitro Characterization of Dendrimer-based Contrast Agents for Magnetic Resonance Imaging

Published on: December 4, 2016

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Area of Science:

Biochemistry
Materials Science
Nanotechnology

Background:

Dendrimers are synthetic, branched nanoparticles with potential in drug and DNA delivery.
Human serum albumin (HSA) is crucial for in vivo transport of compounds and drugs.

Purpose of the Study:

To investigate the interaction between HSA and various dendrimers (mPEG-PAMAM G3, mPEG-PAMAM G4, PAMAM G4).
To analyze binding modes, constants, and conformational changes in HSA upon dendrimer complexation.

Main Methods:

Fourier-transform infrared (FTIR) spectroscopy
UV-visible spectroscopy
Circular dichroism (CD) spectroscopy
Fluorescence spectroscopy

Main Results:

Dendrimers bind to HSA via hydrophilic polypeptide groups.
Binding constants (M⁻¹) were determined for each dendrimer-HSA complex.
Dendrimer complexation induced partial unfolding of HSA, reducing alpha-helix content and increasing random coil/turn structures.

Conclusions:

Dendrimers interact with human serum albumin through hydrophilic binding.
The complexation alters HSA conformation, indicating potential implications for its transport functions.
These findings are relevant for designing advanced dendrimer-based drug delivery systems.