The Nilsson group has a strong interest in understanding and exploiting the principles of molecular recognition that give rise to the defined structure and function of proteins. Protein structure is determined by noncovalent interactions including hydrogen bonding, electrostatic forces, and Van der Waals interactions. The sum of these noncovalent interactions accounts for the observed tertiary and quaternary structure of proteins. A variety of peptides and proteins are known to undergo aggregation and self-assembly as a result of abnormal folding, a process that is characteristic of amyloid diseases, including Alzheimer’s disease (AD), Parkinson’s disease, and diabetes.

The Nilsson group is studying noncovalent interactions in the context of self-assembled peptides in an effort to elucidate the roles of peptide aggregation in disease. We are specifically focused on three areas of study:

1. the characterization of noncovalent side-chain interactions that give rise to protein aggregation and fibril formation, with a focus on the Alzheimer’s disease amyloid-β peptide and other self-assembling peptides;
2. the design of peptides that self-assemble under the control of small molecules or appended oligonucleotide sequences;
3. the development of new methods for the chemical synthesis of proteins using oligonucleotide-templated strategies.

These research efforts utilize the tools of synthetic chemistry and biology to provide a highly innovative and interdisciplinary approach to the study of amyloid proteins.