Recent Developments of Liquid Chromatography Stationary Phases for Compound Separation: From Proteins to Small Organic Compounds

Abstract

Compound separation plays a key role in producing and analyzing chemical compounds. Various methods are offered to obtain high-quality separation results. Liquid chromatography is one of the most common tools used in compound separation across length scales, from larger biomacromolecules to smaller organic compounds. Liquid chromatography also allows ease of modification, the ability to combine compatible mobile and stationary phases, the ability to conduct qualitative and quantitative analyses, and the ability to concentrate samples. Notably, the main feature of a liquid chromatography setup is the stationary phase. The stationary phase directly interacts with the samples via various basic mode of interactions based on affinity, size, and electrostatic interactions. Different interactions between compounds and the stationary phase will eventually result in compound separation. Recent years have witnessed the development of stationary phases to increase binding selectivity, tunability, and reusability. To demonstrate the use of liquid chromatography across length scales of target molecules, this review discusses the recent development of stationary phases for separating macromolecule proteins and small organic compounds, such as small chiral molecules and polycyclic aromatic hydrocarbons (PAHs).

Molecularly Imprinted Affinity Membrane: A Review

“…Protein-selective binding can be used to capture the tagged protein via a specific interaction. 37 For example, a His-tagged protein possessed chelating ligands in amine groups of histidine. This system has been widely applied in protein purification by using affinity chromatography, where nickel(II) ions are adhered to the membrane’s surface.…”

“…Furthermore, recent years have witnessed various affinity membranes specifically developed to target a particular protein. Protein-selective binding can be used to capture the tagged protein via a specific interaction . For example, a His-tagged protein possessed chelating ligands in amine groups of histidine.…”

“…44 Blood proteins, such as albumin and antibodies (immunoglobulins), are typical examples of emerging targets of separation using an affinity membrane. 37 Albumin is selectively adsorbed onto cholic-acid-immobilized poly(2-hydroxyethyl methacrylate) brushes. 46 Polypeptides are also attractive options of affinity ligands for protein separation.…”

A New Mixed‐Mode Stationary Phase Derived from [2‐(3,4‐epoxycyclohexyl)ethyl]trimethoxysilane as a Coupling Reagent and Its RPLC/HILIC/IEC Applications

“…Mixed‐mode stationary phases might have characteristics of high separation selectivity, high loading capacity, and high separation efficiency compared to conventional single‐mode stationary phases [5–7] . Studies on mixed chromatography in the last decade have shown that mixed‐mode chromatography is a versatile approach for the simultaneous separation of highly mixed classes of analytes including highly polar, moderately polar, and nonpolar compounds [8–11] …”

“…[5][6][7] Studies on mixed chromatography in the last decade have shown that mixed-mode chromatography is a versatile approach for the simultaneous separation of highly mixed classes of analytes including highly polar, moderately polar, and nonpolar compounds. [8][9][10][11] The mixed-mode separation mechanism is achieved by using at least two chromatography subtypes together. For example, hydrophobic and hydrophilic interactions are often combined in column chromatography.…”