Molecular Dynamics Simulations of Peptides at the Air–Water Interface: Influencing Factors on Peptide-Templated Mineralization

Biomineralization is the intricate, biomedically highly relevant process by which living organisms deposit minerals on biological matrices to stiffen tissues and build skeletal structures and shells. Rapaport and coworkers (J. Am. Chem. Soc. 2000, 122, 12523; Adv. Funct. Mater. 2008, 18, 2889; Acta Biomater. 2012, 8, 2466) have designed a class of self-assembling amphiphilic peptides that are capable of forming hydrogels and attracting ions from the environment, generating structures akin to the extracellular matrix and promoting bone regeneration. The air–water interface serves both in experiment and in simulations as a model hydrophobic surface to mimic the cell’s organic–aqueous interface and to investigate the organization of the peptide matrix into ordered β-pleated monolayers and the subsequent onset of biomineral formation. To obtain insight into the underlying molecular mechanism, we have used molecular dynamics simulations to study the effect of peptide sequence on aggregate stability and ion–peptide interactions. We findin excellent agreement with experimental observationsthat the nature of the peptide termini (proline vs phenylalanine) affect the aggregate order, while the nature of the acidic side chains (aspartic vs glutamic acid) affect the aggregate’s stability in the presence of ions. These simulations provide valuable microscopic insight into the way ions and peptide templates mutually affect each other during the early stages of biomineralization preceding nucleation