Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.5K
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:
15.5K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

10.8K
10.8K
Ligand Binding Sites02:40

Ligand Binding Sites

15.7K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.7K
Ligand Binding Sites02:40

Ligand Binding Sites

9.0K
9.0K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.9K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.9K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

4.2K
4.2K

You might also read

Related Articles

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

Sort by
Same author

Human Adipose Tissue 11β-Hydroxysteroid Dehydrogenase Type 1 Inhibition Without Tachyphylaxis by Clofutriben, a Pseudo-Irreversible Enzyme Inhibitor.

Clinical and translational science·2025
Same author

Targeting transthyretin in Alzheimer's disease: Drug discovery of small-molecule chaperones as disease-modifying drug candidates for Alzheimer's disease.

European journal of medicinal chemistry·2021
Same author

Optimization of kinetic stabilizers of tetrameric transthyretin: A prospective ligand efficiency-guided approach.

Bioorganic & medicinal chemistry·2020
Same author

Rv0100, a proposed acyl carrier protein in Mycobacterium tuberculosis: expression, purification and crystallization. Corrigendum.

Acta crystallographica. Section F, Structural biology communications·2020
Same author

Antimycobacterial Rufomycin Analogues from <i>Streptomyces atratus</i> Strain MJM3502.

Journal of natural products·2020
Same author

Insights on the Interaction between Transthyretin and Aβ in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.

Journal of medicinal chemistry·2017

Related Experiment Video

Updated: Mar 17, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

30.5K

Ligand Efficiency Indices (LEIs): More than a Simple Efficiency Yardstick.

Cele Abad-Zapatero1,2, Daniel Blasi3

  • 1Center for Pharmaceutical Biotechnology, University of Illinois at Chicago, 900 So. Ashland St, MBRB Building, Room 3020; (M/C870), Chicago, IL 60607-7173, USA. caz@uic.edu.

Molecular Informatics
|July 29, 2016
PubMed
Summary

Ligand Efficiency Indices (LEIs) help assess drug-like molecules by measuring binding affinity per unit size. This study explores LEIs for database analysis, polypharmacology, and fragment-based drug discovery, enhancing medicinal chemistry strategies.

Keywords:
AtlasCBSChemico-biological spaceLEIsLigand efficiency indices

More Related Videos

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
08:40

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

Published on: March 14, 2016

20.4K
Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
11:19

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

11.1K

Related Experiment Videos

Last Updated: Mar 17, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

30.5K
An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
08:40

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

Published on: March 14, 2016

20.4K
Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
11:19

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

11.1K

Area of Science:

  • Medicinal Chemistry
  • Computational Chemistry
  • Drug Discovery

Background:

  • Ligand efficiency is increasingly vital for evaluating drug candidates.
  • Ligand Efficiency Indices (LEIs) quantify binding affinity relative to molecular size (e.g., non-hydrogen atoms or molecular weight).
  • The Atlas of Chemico-Biological Space (AtlasCBS) utilizes LEIs for mapping molecular properties.

Purpose of the Study:

  • To demonstrate novel applications of LEIs in drug discovery.
  • To showcase the utility of AtlasCBS in analyzing and comparing chemical databases.
  • To explore LEI applications in polypharmacology and fragment-based drug design.

Main Methods:

  • Calculation and analysis of Ligand Efficiency Indices (LEIs).
  • Cartesian mapping of chemical and biological space using LEIs (AtlasCBS).
  • Comparative analysis of inhibitor and drug databases.
  • Investigation of polypharmacology and fragment-based strategies using LEIs.

Main Results:

  • LEIs provide a robust method for comparing molecular efficiency across different datasets.
  • AtlasCBS effectively visualizes and differentiates compound sets, aiding database content analysis.
  • LEIs offer insights into polypharmacology and guide fragment-based lead discovery.

Conclusions:

  • The combined use of LEIs and AtlasCBS is a valuable tool for diverse drug discovery applications.
  • LEIs enhance the assessment of compound quality and facilitate strategic decision-making in drug development.
  • This approach promises to advance medicinal chemistry practices and accelerate the discovery of new therapeutics.