Proteins chiral recognition properties

Before starting a preparative chiral separation it is essential to identify a chiral stationary phase (CSP) exhibiting good chiral recognition ability. This is usually done with an analytical column because it is less substance- and time-consuming. A stationary phase mostly composed of silica gel with only a few chiral elements will be rapidly overloaded. In this event, even if the phase exhibits useful properties for analytical purposes, it will not be appropriate for preparative applications this is the case for protein-based phases [102, 103], Most chiral stationary phases have relatively low saturation capacity, so the enantiomer separations are usually done under strongly nonlinear conditions [103], Accordingly, the accurate determination of the adsorption isotherms of the two enantiomers on a CSP is of fundamental importance to allow computer-assisted optimization to scale up the process. 

The recognition of one molecule out of a crowd of many other molecules requires distinction of certain molecular attributes, such as size, polarity, hydrogen bond pattern, chirality, or other physicochemical properties. If several attributes can be checked simultaneously, recognition becomes more selective. Recognition between an enzyme and a substrate was described first by Emil Fischer as the well-known lock and key principle [2], Molecular recognition between complementary DNA strands [3] or protein ligand interactions [4] is very important for the molecular function of living systems. 

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