The chromatographic separation of proteomic standards via a silica immobilized pillararene cavitand has been designed in silico using host–guest binding energy studies and realized experimentally to selectively interact with peptides.

A repetitive sequence of quiescent fluid layers of differing viscosities through which small spherical Brownian particles move is analyzed in order to illustrate in a simple context how the theory of macrotransport processes, a generalization of Taylor dispersion theory, may be employed to rigorously analyze spatially periodic micropatterned chromatographic separation devices for circumstances ...