IAM Drug Discovery Column                                                                       

The IAM.PC phase, developed by Dr. Charles Pidgeon of Purdue University, was the first in a line of IAM phases to be manufactured by Regis. Use of this phase has simplified the inherent difficulties of protein isolation and purification, allowing for rapid purification of membrane proteins while maintaining biological activity. The IAM.PC phase is an important tool for the pharmaceutical industry and academia alike.

The first IAM stationary phase was based on the prevalent membrane lipid, phosphatidylcholine (PC), and consists of monolayers of amphiphilic phospholipids covalently bonded to aminopropyl silica particles through a terminal amide linkage.

The membrane nature of the IAM phase imparts surface characteristics which are useful in the chromatography of membrane proteins. These include: high protein loading, increased protein recovery, recovery of functional activity, and selectivity for membrane proteins.

Large membrane proteins can interact with any combination of polar headgroup, hydrophobic chain, or inner amine groups. The subsurface has been shown to interact with certain solutes, and may or may not contribute to the separation of a given biomolecule. The residual amines can be left unaltered on the subsurface or deactivated through an endcapping procedure, which results in increased stability of the bonded phase. The methyl glycolate endcapping, for example, converts residual amines to neutral amides and introduces a hydroxyl group (IAM.PC.MG).