Elasticity of crystalline beta-sheet monolayers.

Designed amphiphilic beta-sheet peptides with the sequence Pro-Glu-(Phe-Glu)(n)-Pro (n = 2-7) were previously shown by grazing incidence X-ray diffraction (GIXD), to form ordered two-dimensional (2-D) monolayer structures at interfaces induced by the proline residues at peptide termini. The GIXD diffraction pattern was modeled with two coexisting lattice arrangements, suggesting structural flexibility exhibited in the multiple ways by which beta-strands and their amino acid side chains pack into ordered 2-D structures. Here, we find by in-situ GIXD measurements that the ordered beta-sheet assemblies may undergo a quasi-reversible compression and expansion cycle at the air-water interface.