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Supramolecular chemistry is an emerging sub-discipline of chemistry that primarily concerns itself with non-covalent, intermolecular interactions. These relatively weak forces are used in large number to create nanometer sized objects in a massively parallel fashion. The inspiration for this area of research comes primarily from advances in our understanding of biological systems and the miraculous structures found therein. Recently, great strides have been made to mimic both the structures found in biological systems and the approaches that biology uses to create these structures. Our lab uses these non-covalent interactions to direct the self-assembly of novel nanostructured materials. These materials are typically prepared from peptides or peptide derivatives which makes them quick and easy to synthesize. Applications for these materials are diverse. Current projects in our lab include:
- Heterotrimeric Collagen Mimics: Self-assembly of AAB and ABC collagen triple helices. These new peptide assemblies allow us to gain a better understanding of the structure of natural collagen which is often not-homotrimeric. In particular we are interested in the structure of mutations which lead to Osteogenesis Imperfecta and fibrillogenesis.
- Multi-domain peptides self-assemble into nanofibers and can also be triggered to assemble into nanofibrous hydrogels. These materials are used as bioactive, nanostructured materials for tissue engineering, tissue regeneration and drug delivery. The long term goal of this project is the regeneration of entire tissues and organs.
- Application of self-assembled organic materials as templates for the controlled mineralization of inorganics.
- The self-assembly of nanofibrous alpha-helical coiled-coils as a versatile nanostructured scaffold.
- Conversion of alpha-helices to amyloid-like beta sheets and their resulting structure. This is important both in the study of a variety of neurodegenerative diseases (Alzheimer's, Parkinson's, "Mad Cow" etc.) as well as a scaffolding for nanostructure design.
- Design and synthesis of peptides which bind to carbon nanotubes to provide solubility and chemical functionality.
- Design of peptides which bind to the HOX/PBX transcription complex to inhibit cancer growth.
Selected Publications from 2009 - present:
K. M. Galler, L. Aulisa, K. R. Regan, R. N. D'Souza and J. D. Hartgerink "Self-assembling Multidomain Peptide Hydrogels: Designed Susceptibility to Enzymatic Cleavage Allows Enhanced Cell Migration and Spreading" J. Am. Chem. Soc., accepted for publication (2010).
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L. E. Russell, J. A. Fallas and J. D. Hartgerink "Selective Assembly of a High Stability AAB Collagen Heterotrimer" J. Am. Chem. Soc., available online (2010).
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L. Aulisa, H. Dong and J. D. Hartgerink "Self-Assembly of Multidomain Peptides: Sequence Variation Allows Control over Cross-Linking and Viscoelasticity" Biomacromolecules, 10, 2694-2698 (2009).
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J. A. Fallas, V. Gauba and J. D. Hartgerink "Solution structure of an ABC collagen heterotrimer reveals a single-register helix stabilized by electrostatic interactions" J. Biol. Chem., 284 26851-26859 (2009).
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E. L. Bakota, L. Aulisa, D. A. Tsyboulski, R. B. Weisman and J. D. Hartgerink " Multidomain Peptides as Single-Walled Carbon Nanotube Surfactants in Cell Culture" Biomacromolecules, 10, 2201-2206 (2009)
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D. Zhang, O. Neumann, H. Wang, V. M. Yuwono, A. Barhoumi, M. Perham, J. D. Hartgerink, P. Wittung-Stafshede and N. J. Halas "Gold Nanoparticles Can Induce the Formation of Protein-based Aggregates at Physiological pH" Nano Lett. 9, 666-671 (2009).
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L. Aulisa, N. Forraz, C. McGuckin, J. D. Hartgerink "Inhibition of Cancer Cell Proliferation by Designed Peptide-Amphiphiles" Acta Biomaterialia 5, 842-853 (2009).
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