<br/>The area of peptide-based materials has seen a recent surge in interest due to its wide range of potential applications including targeted drug delivery, cancer treatment, tissue engineering, nanoelectronics and batteries. The 20 amino acids, the building blocks of peptides, yields an enormous molecular parameter space which can be used to design peptides with a wide variety of sequences. A fundamental understanding of the impact of peptide sequence on the structure-activity relation of these biological materials will accelerate their development and use, thereby advancing diverse disciplines.<br/><br/>We use a hybrid computational approach, which integrates molecular simulations with analytical techniques, cyber-infrastructure tools and workflows-based methods, to study and develop new biological materials with desired sequence-structure-activity properties in a more time- and cost-efficient way. We will also use Replica Exchange to aid with the development of a sequence-structure-activity phase diagram. The biological materials are formed via the self-assembly of amphiphilic ultrashort peptides encompassing aromatic amino acids (namely, diphenylalanine and phenylalanine-asparagine-phenylalanine). The extended spatiotemporal scales connecting molecules to materials is addressed via the use of coarse-grained representations of the molecular species (S. Mushnoori, et al Organic & Biomolecular Chemistry 2018, 16, 2499). The dynamics underlying the self-assembly of these peptides is resolved via the classical Molecular Dynamics simulation method.

Ultrashort peptide materials design via a hybrid computational approach

2019 Spring National Meeting

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