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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
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An N-terminus with small acidic motif (DSpSpEE) that is also found in SIBLING proteins [65]. When solubilized, statherin has a random coil conformation. When bound to HA, it takes on a more alpha-helical structure exposing a bacterial binding site [63], leading to bacterial entrapment. Another example is the role of the IDP, DMP1, in preventing kidney and cardiovascular calcification. The double k
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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