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

Ligand Binding and Linkage

Ligand Binding and Linkage

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...

Ligand Binding and Linkage

Ligand Binding and Linkage

Ligand Binding Sites

Ligand Binding Sites

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...

Ligand Binding Sites

Ligand Binding Sites

Metal-Ligand Bonds

Metal-Ligand Bonds

The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...

The Equilibrium Binding Constant and Binding Strength

The Equilibrium Binding Constant and Binding Strength

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:

You might also read

Related Articles

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

Sort by

Same author

De Novo Discovery of Prenylated Macrocyclic Peptide Ligands.

Methods in molecular biology (Clifton, N.J.)·2026

Same author

<i>De Novo</i> Boronic Acid-Containing Macrocyclic Peptides That Selectively Bind a Sialylated <i>N</i>-Glycan.

Journal of the American Chemical Society·2026

Same author

Post-Translational Aldehyde-Mediated Backbone Alkylation Enables Constrained α-Amino-γ-Lactam Motifs in mRNA Display.

Journal of the American Chemical Society·2026

Same author

A RaPID Macrocyclic Peptide Inhibitor of ROR1/2 Strongly Reduces Proliferation of Diffuse Intrinsic Pontine Glioma Cells.

ACS chemical biology·2026

Same author

Development and structure-guided characterization of a novel ACE2-binding macrocyclic peptide.

Journal of structural biology: X·2026

Same author

The Alteromonas macleodii ribosome enables consecutive incorporation of bulky D-amino acids into peptides.

Nucleic acids research·2026

Search research articles

Related Experiment Video

Updated: Feb 1, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

Structural Features and Binding Modes of Thioether-Cyclized Peptide Ligands.

Manuel E Otero-Ramirez¹, Toby Passioura², Hiroaki Suga^3,4

¹Department of Chemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, 113-0033 Tokyo, Bunkyo-ku, Japan. motero@chem.s.u-tokyo.ac.jp.

|December 16, 2018

Summary

Macrocyclic peptides offer potent therapeutic potential. This review details thioether-closed macrocyclic peptide structures, crucial for understanding their target binding and therapeutic applications.

Keywords:

crystallography macrocyclic peptide

More Related Videos

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

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

Published on: March 14, 2016

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Related Experiment Videos

Last Updated: Feb 1, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

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

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

Published on: March 14, 2016

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Area of Science:

Medicinal Chemistry
Structural Biology
Biochemistry

Background:

Macrocyclic peptides are a promising class of therapeutic compounds due to their high potency, affinity, and selectivity.
Recent advancements in biochemical techniques have enabled the isolation of high-affinity macrocyclic peptides.
Thioether formation is a common method for macrocyclization in these identified compounds.

Purpose of the Study:

To review target-bound thioether-closed macrocyclic peptide structures.
To provide insights into the structural conformation and target-binding mechanisms of these peptides.

Main Methods:

Literature review of identified bioactive macrocyclic peptides.
Analysis of x-ray crystallographic data for macrocyclic peptide-target complexes.

Main Results:

Compilation of various target-bound thioether-closed macrocyclic peptide structures.
Detailed structural information on peptide conformation and binding modes.

Conclusions:

Thioether-closed macrocyclic peptides represent a significant area of therapeutic development.
Structural insights from x-ray crystallography are vital for optimizing macrocyclic peptide drug design.