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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...
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...
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,...
Physical Properties of Amines01:26

Physical Properties of Amines

Amines with low molecular weight are usually gaseous at room temperature, while those with high molecular weight are liquid or solids in nature. Usually, low molecular weight amines have a rotten fish-like smell. Diamines typically have a pungent smell. For instance, cadaverine and putrescine, depicted in Figure 1, are two molecules responsible for decaying tissue.
Factors Affecting Protein-Drug Binding: Patient-Related Factors01:29

Factors Affecting Protein-Drug Binding: Patient-Related Factors

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...

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Related Experiment Video

Updated: Jul 11, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
08:26

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)

Published on: August 31, 2018

Polyamine analogues bind human serum albumin.

R Beauchemin1, C N N'soukpoé-Kossi, T J Thomas

  • 1Département de Chimie-Biologie, Université du Québec à Trois-Rivières, C P 500, Trois-Rivières (Québec), Canada.

Biomacromolecules
|September 25, 2007
PubMed
Summary

This study investigated how polyamine analogues interact with human serum albumin (HSA). Polyamines bind to HSA, altering its structure and potentially influencing drug delivery for cancer therapy.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Polyamine analogues exhibit antitumor activity and modulate chemotherapy efficacy in breast cancer.
  • Polyamines interact with nucleic acids and proteins as part of their mechanism of action.

Purpose of the Study:

  • To investigate the interaction between human serum albumin (HSA) and synthetic polyamine analogues.
  • To determine the binding mode and structural impact of polyamine analogues on HSA.

Main Methods:

  • Utilized Fourier-transform infrared (FTIR), UV-visible, and circular dichroism (CD) spectroscopy.
  • Analyzed interactions in aqueous solution at physiological conditions with varying polyamine concentrations.

Main Results:

  • Polyamines bind non-specifically to HSA via hydrogen bonding with polar groups.
  • Binding constants were determined: K333 = 9.30 x 10(3) M(-1), KBE-333 = 5.63 x 10(2) M(-1), KBE-3333 = 3.66 x 10(2) M(-1).
  • HSA secondary structure significantly altered, with decreased alpha-helix (55% to 43-50%) and increased beta-sheet (17% to 29-36%), indicating partial unfolding.

Conclusions:

  • Polyamine analogues interact with HSA, causing structural changes indicative of partial unfolding.
  • HSA structure was less affected by these analogues compared to biogenic polyamines.
  • Understanding these interactions is crucial for developing polyamine-based cancer therapies.