In 2008, Alpert coined the term, ERLIC (electrostatic repulsion hydrophilic interaction chromatography), for HILIC separations where an ionic column surface chemistry is used to repel a common ionic polar group on an analyte or within a set of analytes, to facilitate separation by the remaining polar groups. Electrostatic effects have an order of magnitude stronger chemical potential than neutral polar effects. This allows one to minimize the influence of a common, ionic group within a set of analyte molecules; or to reduce the degree of retention from these more polar functional groups, even enabling isocratic separations in lieu of a gradient in some situations. His subsequent publication further described orientation effects which others have also called ion-pair normal phase or e-HILIC, reflecting retention mechanisms sensitive to a particular ionic portion of the analyte, either attractive or repulsive. ERLIC (eHILIC) separations need not be isocratic, but the net effect is the reduction of the attraction of a particularly strong polar group, which then requires less strong elution conditions, and the enhanced interaction of the remaining polar (opposite charged ionic, or non-ionic) functional groups of the analyte(s).Based on the ERLIC column invented by Andrew Alpert, a new peptide mapping methodology was developed with unique properties of separation of asparagine deamidation and isomerization. This unique properties would be very beneficial for future mass spectrometry based multi-attributes monitoring in biologics quality control.