Scientific Achievement
A series of peptide amphiphiles that assemble into one-dimensional nanostructures was explored. Determinations were made on how the length of the peptide sequence and the identity of the hydrophobic amino acid impact the heme binding affinity, heme density, and the electronic properties.
Significance and Impact
The results are applicable to the design of 1D peptide assemblies reminiscent of natural structures. Such structures would have potential utility as supramolecular bioelectronic materials useful in biomedical sensing and as enzymatic materials.
Research Details
With sequence length of n = 2, the peptide assembly yielded the greatest binding affinity. The resulting nanoscale assemblies produced ordered arrays of the redox active molecule heme.
Work was performed at the Center for Nanoscale Materials.
DOI: 10.1039/D2NR00473A
About Argonne’s Center for Nanoscale Materials
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