Related Experiment Video

Updated: Jan 12, 2026

Spatiotemporally Controlled Nuclear Translocation of Guests in Living Cells Using Caged Molecular Glues as Photoactivatable Tags
10:10

Spatiotemporally Controlled Nuclear Translocation of Guests in Living Cells Using Caged Molecular Glues as Photoactivatable Tags

Published on: January 17, 2019

11.3K

Revealing Pathway Complexity in Host-Guest Binding: Allosteric Regulation and Temporal Chiral Inversion During

Long Chen1, Xiaotong Liang1, Pinyou Wang1

  • 1Key Laboratory of Green Chemistry and Technology of the Ministry of Education, College of Chemistry, and State Key Laboratory of Biotherapy, Sichuan University, Chengdu, 610064, China.

Angewandte Chemie (International Ed. in English)
|November 4, 2025
PubMed
Summary

This study reveals novel chiral inversion kinetics in host-guest complexation using Naphtho[n,n]urils (NGU[n,n]). Complexation induces conformational changes and chiral allosteric regulation, offering new insights into supramolecular chemistry.

Keywords:
Allosteric regulationChirality inversionHost–guest ComplexationMacrocyclesPathway complexity

More Related Videos

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes07:22

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

4.4K
Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

14.9K

Related Concept Videos

Ligand Binding and Linkage00:49

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...
5.5K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.5K
Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
1.2K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.6K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
8.6K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

3.0K