Hierarchical Assembly of Peptide Materials

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With the support of the Macromolecular, Supramolecular and Nanochemistry Program in the Division of Chemistry, Professor Jean Chmielewski of Purdue University will conduct research building unique structures on a nano- to micro-scale using ball and stick atomic and molecular building blocks. Professor Chmielewski will study how the size and shape of the prepared structures can be controlled by changing the building blocks at a molecular level. These nano- and micro-structures will be developed to ultimately encapsulate protein drugs for delivery to cells, and to make self-healing materials. Professor Chmielewski will continue to diligently train chemistry students and work toward improving the diversity of the chemistry graduate student population at Purdue University. In this way a new generation of diverse scientists will be available to tackle the technological challenges of the 21st century.Gaining a fundamental understanding of the interactions between nanomaterials and biopolymers, such as proteins and nucleic acids, would have a broad impact on a number of applications, from tissue engineering to device fabrication. Overall, the experiments to be conducted under this award seek to expand supramolecular assembly to the study of peptide-based biomaterial hosts with biopolymer guests and examine cells and as self-replicating materials. The intellectual merit of the proposed studies is focused on gaining a firm understanding of the parameters and mechanisms of macromolecular supramolecular assembly within peptide crystals, nanotubes and nanospheres. At the end of the proposed funding period, the Chmielewski team aims to have optimized conditions for the generation of distinct peptide nano- and microstructures on demand and a basic understanding of the mechanistic underpinnings of the supramolecular assembly process. Key areas of study include the interaction of the peptide nano- and microstructures with biopolymers, and their interactions with cells, and self-replication of these peptide-based structures.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.