LAUSR

This paper reports the dynamic interfacial behavior of a new interfacially active peptide AM-S, which was designed based on a peptide surfactant AM1 modularized with an additional silk-derived hydrophobic tail to enhance anchoring to air–water interfaces. AM-S peptide shows a random coil conformation in bulk solution similar to AM1 as determined by circular dichroism spectroscopy, which facilitates rapid adsorption at the air–water interface, reducing interfacial tension from 72 to 52 mN/m within 300 s at a low concentration of 10 μM. Although the interfacial films formed by AM-S demonstrated low tensile stress as compared to AM1, the AM-S films in the presence of Zn(II), but not in its absence, show significant resistance against compression, as peptides were unable to desorb quickly under the compression conditions imposed by the Cambridge interfacial tensiometer (CIT). These results indicate that AM-S peptides tend to undergo a multilayer adsorption at the interfaces, in contrast to AM1 peptide that on...