A robust protein-mimicking metallo-amine cage showing proton-driven allostery with water as the effector
Yu‐Lin Lu, Xiaodong Zhang, Yu-Han Qin, Jiaqi Song, Yin‐Hui Huang, Chenhui Liu, Jingjing Chen, Hai‐Sen Xu, Mei Pan, Cheng‐Yong Su
Abstract
The allosteric effect is omnipresent in proteins with two distinct binding sites communicating over a distance to control biological functions and complex processes, which drives an everlasting innovation of molecular-scale devices and machines with allosteric functions. Herein, we report a protein-mimicking metallo-amine cage (MOC-68) with excellent tolerance for harsh acid-base conditions, presenting a proof-of-concept example of proton-driven allosteric regulation of multi-state transitions and molecular motions controlled by a water effector as in the natural system. Owing to its multiple N groups for proton transfer, 8 water-binding allosteric sites for remote control, and one endo-cavity and six exo-cavities for guest exchange, the acid-base or solvent switching protocols of cage conformation, charge-state, amphoteric property, phase transfer, guest dynamics, and, unprecedentedly, ring-on-cage sliding and capping/uncapping motions have been demonstrated; this not only provides a unique allosteric cage model for molecular machines and smart biomaterials but also promises potential in drug delivery and release.