A survey of the different roles of polyoxometalates in their interaction with amino acids, peptides and proteins

Abstract

One of the most attractive areas in inorganic chemistry is the synthesis of polyoxometalates (POMs) exhibiting new properties and applications. Since the impact of POMs in biochemistry and related fields of research has increased in the last few years, there has been a special interest in this topic. Significant progress in biological applications has been made where the interaction of POMs with amino acids, peptides and proteins is relevant. Versatile POMs play a series of different roles in the interaction with these biomolecules as described in this review. Various types of interactions are established, depending on the POM shape and charge, the amino acid side chain, peptide sequence or protein structure. Experimental conditions such as temperature, acidity, solvent, etc. are also important factors that influence the binding/reactivity of POM with biomolecules, as described herein. This understanding allows the adequate design of the POM-biomolecule couple for tailoring and controlling mechanisms of action such as catalysis, inhibition, and aggregation, or the crystallising agent.

Complexes of Keggin POMs [PM12O40]3– (M = Mo, W) with GlyGly Peptide and Arginine – Crystal Structures and Solution Reactivity

“…The individual oligonuclear oxo‐hydroxo complexes are generally denoted by a term Poly‐oxo‐metalates (POMs). In the literature there are available a number of examples of protein and peptide complexes of POMs, derived mostly from the most acidic oxo‐vanadic and oxo‐molybdic acids. Characterization of their bonding to peptides has never been the major aim of the structure studies even if a number of reviews has recently drawn the attention to this aspect , …”

“…Characterization of their bonding to peptides has never been the major aim of the structure studies even if a number of reviews has recently drawn the attention to this aspect. [15,16] We felt thus a challenge to produce a comparison of structure and reactivity of the complexes of structurally identical but chemically different POMs with simple peptide and amino acid model substances. Here, we report the results of interaction of simple Keggin POMs derived from Mo and W with the structurally simplest peptide glycylglycine, GlyGly, and amino acid arginine, Arg, often present as fragments in specific binding sites of proteins.…”

Synthesis and biological activity of an Anderson polyoxometalate bis‐functionalized with a Bombesin‐analog peptide

“…Peptides are suitable pendants for POMs and can be covalently grafted via amide bonds . On the other hand, as observed for the targeted proteins mentioned above, they can also establish multiple weak interactions with the POM surface, being these usually more efficient upon increasing of size and charge density of the polyanion, or when using transition metal‐substituted POMs with free coordination positions on the metal ions …”

Transition Metal Substituted Polyoxometalates as α‐Glucosidase Inhibitors

“…In addition, POMs are also used in protein crystallography. [28,29] Polyoxometalates have made great achievements in the field of enzyme inhibitors. It is reported that polyoxometalates have significant effects on the activities of nucleosidase, phosphatase, sulfate transferase, sialic acid transferase, acetylase, nuclease and protease.…”