Self‐Assembling Catalytic Peptide Nanomaterials Capable of Highly Efficient Peroxidase Activity

Abstract

The self‐assembly of short peptides gives rise to versatile nanomaterials capable of promoting efficient catalysis. We have shown that short, seven‐residue peptides bind hemin to produce functional catalytic materials which display highly efficient peroxidation activity, reaching a catalytic efficiency of 3×105 m−1 s−1. Self‐assembly is essential for catalysis as non‐assembling controls show no activity. We have also observed peroxidase activity even in the absence of hemin, suggesting the potential to alter redox properties of substrates upon association with the assemblies. These results demonstrate the practical utility of self‐assembled peptides in various catalytic applications and further support the evolutionary link between amyloids and modern‐day enzymes.

De novo designed peptides form a highly catalytic ordered nanoarchitecture on a graphite surface

“…To test our hypothesis, we employed several peptides from a recent report. 31 These peptides were found to self-assemble in the presence of hemin into catalytic amyloids with high peroxidation activities in solution. Among them, we selected highly active (LMLHLFL and LILHLFL) and moderately active (LHLHLFL and VHVHVYV) peptides in this work ( Fig.…”

Systems chemistry of peptide-assemblies for biochemical transformations

“…Notably, the slight modification in sequence (Ac-LMLHLFL-NH 2 ) resulted in peroxidase activity that reaches up to 3 Â 10 5 M À1 s À1 at pH 6, thus foreshadowing the significance of catalytic promiscuity of these peptide sequences towards evolutionary journey of modern enzymes. 156 Jelinek and co-workers utilized a naturally occurring amyloid b peptide (Ab42) to achieve different catalytic activities (Fig. 9b).…”

“…[134][135][136][137][138][139][140][141][142] Intriguingly, the proper selection and the orientation of these different functional amino acid residues such as lysine, histidine, and tyrosine in the self-assembled state can show promiscuous activity as well as cascade transformations, thus emulating advanced traits of modern enzymes. [148][149][150][151][152][153][154][155][156][157][158][159][160][161][162][163][164][165] Apart from functional residues, morphological variation has been shown to play a significant role in altering the catalytic activity. However, it is not straightforward to predict the morphology dependent activity of minimal peptide building blocks due to the variability of exposed catalytic sites as well as the nature of binding grooves.…”

“…Notably, the slight modification in sequence (Ac-LMLHLFL-NH 2 ) resulted in peroxidase activity that reaches up to 3 × 10 5 M −1 s −1 at pH 6, thus foreshadowing the significance of catalytic promiscuity of these peptide sequences towards evolutionary journey of modern enzymes. 156…”

“…134–142 Intriguingly, the proper selection and the orientation of these different functional amino acid residues such as lysine, histidine, and tyrosine in the self-assembled state can show promiscuous activity as well as cascade transformations, thus emulating advanced traits of modern enzymes. 148–165…”