Title : Insights into non-natural peptide aggregation: Accelerated molecular dynamics (amd) for biocompatible material design
Abstract:
In the last year, an increasing interest has been observed toward the design of small molecules that can self-assemble to form supramolecular structures. In particular, peptides gain attention due to their unique qualities like being friendly to living organisms, conducting electricity well, having various shapes and properties, being strong, and being easy to synthesize in large quantities. Natural peptides are good biocompatible materials but have some drawbacks like limited structural diversity, biological instability, variable biocompatibility, variable self- assembly and limited scalability. Peptides made with non-natural amino acids can overcome the limited structure diversity which restrict range of supramolecular structures, biological stable, having biocompatibility with consistent and reliable self-assembly behavior and large scalability. We recently investigated the supramolecular aggregation of peptides containing the fluorinated beta-amino acid able to form a conductive rope. We are now analyzing the aggregation behavior of new tetrapeptides composed by L-alanine, Fpg, and the chlorinated beta-amino acid Clpg. The four peptides have the same composition but differ in stereochemistry. The conformational behavior of these designed tetrapeptides was studied by accelerated molecular dynamics simulations. The results shows that the peptides have mostly a bend- shape folding, with a radius of gyration between 4.4 and 4.6 Å.
