Synthesis of Peptide-Amphiphiles for Binding Inorganic Molecules

Constructing biomaterials capable of mimicking reactions and processes specific to certain proteins is a challenging endeavor of interest to many researchers. The development of peptide-amphiphiles that combine amphiphilic properties with specific bioactivity has made it possible to synthesize molecules that self-assemble to mimic protein function. This research involves synthesizing peptide-amphiphiles with a peptide head group capable of folding into the native structure of a protein involved in the condensation of bone, attached to a monoalkyl tail. The peptide-amphiphiles created were then characterized and examined to see how they self-assembled in solution and whether they displayed any specific bioactivity related to their head group molecular architecture. Analyzing the peptide-amphiphiles’ structures was done by observing circular dichroism spectras, while collecting and characterizing the peptide-amphiphiles was done using HPLC (high performance liquid chromatography), MALDI-TOF MS (matrix-assisted laser desorption ionization time-of-flight mass spectrometry) and NMR (nuclear magnetic resonance). This research has far-reaching applications in synthesizing inorganic materials found in the body such as bone and helping to treat diseases where inorganic materials are involved.