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Related Concept Videos

Protein Absorption01:12

Protein Absorption

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Proteins in the gastrointestinal tract typically come from food, but they can also originate from disintegrated cells or secreted enzymes. In the stomach, the enzyme pepsin breaks down these proteins into polypeptides. The fragments then move into the duodenum as a semi-fluid mass called chyme. Pancreatic proteases, such as trypsin and chymotrypsin, and intestinal brush border enzymes like carboxypeptidases further dismantle the polypeptides into tripeptides, dipeptides, and free amino acids.
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Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

Factors Affecting Protein-Drug Binding: Protein-Related Factors

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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

The Equilibrium Binding Constant and Binding Strength

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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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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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Drug Distribution: Plasma Protein Binding01:29

Drug Distribution: Plasma Protein Binding

8.8K
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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Protein-Drug Binding: Mechanism and Kinetics01:16

Protein-Drug Binding: Mechanism and Kinetics

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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,...
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Updated: Jan 28, 2026

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Label-Free and Immobilization-Free Protein-Binding Assays by Ultraviolet Transient Absorption Microscopy.

Jianghao Shen1, Qiangqiang Wang2, Fan Wu1

  • 1Institute of Medical Photonics, Beijing Advanced Innovation Center for Biomedical Engineering, School of Biological Science and Medical Engineering, Beihang University, Beijing, China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|January 27, 2026
PubMed
Summary

We developed ultraviolet transient absorption microscopy (UV-TAM) for label-free protein-ligand interaction studies. This method directly detects binding in solution, offering a new tool for drug discovery.

Keywords:
label‐free detectionprotein‐ligand interactionsultraviolet transient absorption

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Area of Science:

  • Biochemistry
  • Biophysics
  • Analytical Chemistry

Background:

  • Protein-ligand interactions are crucial for biological processes and drug development.
  • Traditional methods for studying these interactions often require labeling or immobilization, which can interfere with natural binding behaviors.

Purpose of the Study:

  • To introduce ultraviolet transient absorption microscopy (UV-TAM) as a novel, label-free technique for studying protein-ligand interactions in solution.
  • To demonstrate the utility of UV-TAM for real-time detection of binding events and quantitative analysis.

Main Methods:

  • Utilized femtosecond deep-UV laser pulses for excitation and a near-UV probe beam to monitor changes in tryptophan residue excited-state dynamics.
  • Employed UV-TAM for label-free, in-solution measurements of protein-ligand binding using microliter sample volumes.
  • Applied the technique to study interactions between plasma proteins (bovine serum albumin, hemoglobin) and alkaloid ligands (berberine, palmatine).

Main Results:

  • UV-TAM successfully detected binding events through ligand-induced alterations in time-resolved spectral dynamics.
  • Quantitative analysis of hemoglobin-alkaloid interactions provided dissociation constants that closely matched those obtained via isothermal titration calorimetry.
  • Demonstrated the label-free and in-solution capabilities of the UV-TAM technique.

Conclusions:

  • UV-TAM offers a robust, calibration-free platform for the direct detection and quantification of protein-ligand interactions in solution.
  • The technique shows significant potential for advancing biochemical research and facilitating high-throughput drug discovery screening.