1
Ptide absorbed to CAP was consistent with an -helix, whereas when bound to HA the structure corresponded more to a random coil [107]. We studied DPP peptides by FTIR spectroscopy and found the phosphorylated peptides in solution in the presence of HA formed -helical structures and lost their random coil characteristics [108]. Perhaps, through evolution, the most efficient strategy found by nature
1
Ns [102, 106]. In contrast, IDPs are charged proteins, thus they can control their interfacial absorption onto solid surfaces [106]. Experiments, in silico, suggest that intrinsically disordered peptides absorbed to a surface with a complementary pattern form a well-defined structure (-helix) indicating that a specific surface can stabilize the structure of an IDP peptide. The effect of a compleme