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The biological activity of the selected peptides from the combinatorial library in bacteria, fungi and mammalian cells is studied to characterize the selected peptides and to compare the activity of antimicrobial peptides (AMPs) in vitro and in vivo. The analysis has shown that the methods focusing on screening peptide libraries in vitro for membranes with the appropriate interfacial activity has enabled the design, selection and discovery of novel, potent and broad-spectrum membrane-active antibiotics.

A nonclassical approach is used for biomolecular engineering and design of membrane-active peptides. The composition-space peptide libraries coupled with function-based high-throughput screens has led to the discovery of diverse, soluble and highly potent membrane-permeabilizing peptides.

Beta sheet pore forming peptides are characterized and the structure function relationships in lipid vesicles are compared to their activity in biological membranes. Fluorescence spectroscopy and quenching showed that the peptides reside mainly on the bilayer surface and are partially exposed to water, rather than in a membrane-spanning state.