The Nilsson Group

Peptide Self-Assembly: Pathology to Engineered Biomaterials

Journal of the American Chemical Society Cover

The Nilsson group studies the fibril self-assembly of β-sheet peptides in order to understand protein-misfolding disorders and to create novel biomaterials. The self-assembly of peptides and proteins into cross-β amyloid structures is a defining characteristic of amyloid pathologies including Alzheimer's disease, Parkinson's disease, type 2 diabetes, and prion encephalopathies. Amyloid protein assemblies are not limited to pathological conditions, but also exist as evolutionarily conserved motifs with defined biological function. There is growing interest in exploiting peptide self-assembly phenomena for the development of novel functional structures with applications in biomedicine, energy, and materials. The long-term goals of the Nilsson group are to understand the noncovalent interactions that drive peptide self-assembly in order to facilitate novel approaches to perturb and control these processes and to exploit these interactions to enable new strategies for the noncovalent synthesis of functional and dynamic self-assembled materials.

Research in the Nilsson group is highly interdisciplinary and exists at the interface between organic, biological, and materials chemistry. We exploit techniques in organic synthesis to create novel peptide-based agents that self-assemble into amyloid-inspired architectures. The self-assembly of these peptides is studied by extensive biophysical analysis. Finally, the emergent, higher-order properties of these self-assembled materials are characterized in order to understand their suitability as functional biomaterials. We also conduct studies of pathological amyloid peptides, including the Alzheimer's disease amyloid-β peptide and SEVI fibrils that influence the infectivity of HIV. We characterize the self-assembly mechanisms of these peptides with a special interest in understanding the nature of prefibril oligomer structures.

Figures are covers that feature work from the Nilsson group (J. Am. Chem. Soc. 2010, 132, 9526–9527; Polym. Chem. 2012, 3, 18–33).

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