Reconfigurable Mechanically Interlocked Metal-Organic Nanocages for Adaptive Guest Recognition and Allosteric

Dongpu Wu1, Zheng Li1,2, Yong-Kang Zhu1

  • 1College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun 130012, P. R. China.

ACS Nano
|March 18, 2026
PubMed
Summary

Researchers created a reconfigurable nanocage that mechanically interlocks to form a dimer. This adaptive nanostructure exhibits selective molecular recognition and allosteric responses, mimicking biological systems for advanced applications.

Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
64.3K
Allosteric Regulation01:08

Allosteric Regulation

16.1K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.8K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

3.2K
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...
9.3K
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...
6.9K