The self-assembly of peptides has been extensively studied over the past three decades. Through these studies, a multitude of nano- and biotechnological applications has been devised. Most of these studies center on the use of a single self-assembling peptide to confer a desired property. In principle, it is possible to design a multifunctional peptide that can (1) undergo self-assembly into the desired macromolecular structure and (2) display the functional groups that will confer the desired properties upon the peptide material. However, this will almost necessitate a complex synthesis of the multifunctional peptide while juggling the different chemistries of the functional groups. Another approach that might be more feasible, and is gaining popularity, is the co-assembly of different molecules to furnish a complex macromolecule with desired properties. In nature, this is manifest in the assembly of various enzymes, e.g. the tRNA ligase, from their component polypeptide moieties. Currently, however, studies on the co-assembly of peptides are still limited. In this talk, I discuss our initial studies into the utility of a common pentapeptide backbone to mediate the co-assembly of analogous hexapeptides with different C-terminal amino acids. Using a combination of circular dichroism (CD) spectroscopy, attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy, and transmission electron microscopy, we have been able to infer that the co-assembly of hexapeptides with a common backbone can indeed transpire, but that this is dependent to a small extent on the C-terminal amino acids. This represents the first step in elucidating the structure-co-assembly relationship among the oligopeptides towards the bottom-up fabrication of a complex peptide material.

Mediation of co-assembly of peptides with different functionalities via a common peptide backbone

ACS Spring Meeting 2021

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