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Investigating Biological tuning of synthetic tactics in solid-phase synthesis: application to ABeta (1-42) is discussed. Furthermore having demonstrated a hitherto-unreported on-resin reduction of the sulfoxide 'aggregation protecting group' to allow for standard cleavage protocols, obviating a separate solution-phase sulfoxide reduction step.

The use of baculoviral polyhedrin (Polh) protein as a novel fusion partner for the production of a model antimicrobial peptide (AMP) in Escherichia coli is investigated. Results demonstrate that baculoviral Polh can provide an efficient and facile platform for the production or functional study of target AMPs.

The majority of the cell-penetrating peptides (CPPs) are designed on the basis of known, naturally occurring peptides and proteins that meditate physiological membrane processes such as fusion, disruption, and pore formation. Symmetrical disulfade-linked dimer is the first CPP whose specific membrane translocation mechanism is controlled by a dimerization dependent 'switch'.