In contrast to well established, commercially available peptide species, we concentrate our studies on a recently reported peptide model that was designed for spanning the membrane hydrophobic core and anchoring at the membrane/water interface. Therefore, this motif holds a tunable, conformationally stable peptide structure that is open for multiple functionalization ). The D,L alternation of the peptide backbone concordant with a double-helical b-type shape is related to natural peptide antibiotics such as gramicidin A (Kelkar and Chattopadhyay 2007) or feglymycin (Bunkóczi et al. 2005) . In addition, the studied sequences are unique on their own due to their almost purely aromatic side-chain composition (Alexopoulos et al. 2004; Küsel et al. 2007 ).