# Binding Zinc and Oxo-Vanadium Insulin-Mimetic Complexes to Phosphatase Enzymes: Structure, Electronics and Implications

## TL;DR

This paper studies how insulin-mimetic zinc and vanadium complexes bind to phosphatase enzymes, focusing on their structure and electronic properties in different environments.

## Contribution

The study introduces a combined computational approach to analyze metal complex binding to phosphatases, integrating AI for biomedical and quantum applications.

## Key findings

- Vanadyl and zinc complexes show similar ionic radii and coordination geometry in aqueous environments.
- Protein embedding alters the electronic states of metal centers, affecting binding behavior.
- AI-assisted methods can enhance the design of metal-based insulin mimetics for biomedical use.

## Abstract

We explore the structural and electronic properties of representative insulin-mimetic oxovanadium and zinc complexes as computed in vacuum, in water clusters and upon binding to PTEN and PTP1B phosphatases. Albeit diverse, the enzymes’ active sites represent evolutionary variant choices of the same type of biochemistry. Though different in respect to covalency and the orbital nature of bonding, theory predicts comparable ionic radii, bond lengths and square pyramidal coordination for the considered vanadyl and zinc systems when in an aqueous environment. Employing docking, DFT and quantum mechanics/molecular mechanics methods, we address possible polar interactions in the protein environments and compute infrared/Raman modes and optical electronic properties, which may be suitable for the structural analysis of the specific chemical moieties in binding studies. Accounting for how protein embedding may alter the electronic states of metal centres, we discuss artificial intelligence-assisted protein field engineering to assist biomedical and quantum information applications.