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Sugar-coated Peptoid Nanosheets Selectively Detect Multivalent Proteins
A team led by Foundry researchers has developed a method to engineer the surface of peptoid nanosheets, mimicking some of the properties of cell membranes, to interact with multivalent proteins.
Significance and Impact
This is the first time that nanostructures have been engineered with such sophistication that they approach the structural precision and complexity that found in nature. The new method will enable materials that can selectively detect proteins, and potentially viruses and cells, for use in biosensors, therapeutics, or the bioremediation of threat agents.
- Taking advantage of the known affinity of many proteins for carbohydrates, the researchers functionalized the surface of peptoid nanosheets with a variety of simple sugars.
- The sugars were attached to the nanosheet using compounds of different lengths or within loops.
- With imaging tools at the Molecular Foundry and support from the Advanced Light Source, the researchers confirmed the structure and biological function of the glycosylated peptoid nanosheets.
- The researchers demonstrated that the glycosylated peptoid nanosheets were capable of selectively binding a variety of proteins, including Shiga toxin subunit B.
A. Battigelli, J.H. Kim, D.C. Dehigaspitiya, C. Proulx, E.J. Robertson, D.J. Murray, B. Rad, K. Kirshenbaum, R.N. Zuckermann. ACS Nano. Article ASAP (2018). DOI: 10.1021/acsnano.7b08018