The self-assembly of a tripeptide into particles with different morphologies is described along with the particles application as antibiofouling and antimicrobial coatings.
The COVID-19 pandemic highlighted the importance of developing surfaces and coatings with antiviral activity. Here, we present, for the first time, peptide-based assemblies that can kill viruses. The minimal inhibitory concentration (MIC) of the assemblies is in the range tens of micrograms per milliliter. This value is 2 orders of magnitude smaller than the MIC of metal nanoparticles. When applied on a surface, by drop casting, the peptide spherical assemblies adhere to the surface and form an antiviral coating against both RNA-and DNA-based viruses including coronavirus. Our results show that the coating reduced the number of T4 bacteriophages (DNA-based virus) by 3 log, compared with an untreated surface and 6 log, when compared with a stock solution. Importantly, we showed that this coating completely inactivated canine coronavirus (RNA-based virus). This peptide-based coating can be useful wherever sterile surfaces are needed to reduce the risk of viral transmission.
What do you consider to be the exciting developments in the field?We demonstrated the catalytic activity of the non-coded amino acid DOPA. In some cases, DOPA performed better than the coded amino acid His. We believe that this finding on a noncoded amino acid can advance the area of prebiotic catalysis. Hopefully, it will lead to a better understanding of enzyme's evolution.
Better understanding how reactions have been catalyzed in the prebiotic world is important for better realizing how enzymes have evolved. The dominant hypothesis is that the first catalyst was an RNA molecule. It was also assumed that amyloid fibrils, self‐assembled by peptides or proteins, served as the first catalysts. However, debate still exists regarding which process occurred first: the polymerization of RNA or the synthesis of proteins. Here, we show that an individual amino acid, L‐3,4‐dihydroxyphenylalanine (DOPA), can act as a catalyst. This amino acid is the main constituent of mussel adhesion proteins that function in harsh conditions very similar to plausible prebiotic conditions. By tracing the hydrolysis of two compounds, p‐nitrophenylacetate and acetylcholine, we showed that DOPA catalyzes a reaction; we suggest its role as a prebiotic catalyst.
Antiviral compounds are important for generating sterile surfaces. Here, two extremely short peptides, DOPA‐Phe‐NH2 and DOPA‐Phe(4F)‐NH2 that can self‐assemble into spherical nanoparticles with antiviral activity are presented. The peptide assemblies possess excellent antiviral activity against bacteriophage T4 with antiviral minimal inhibitory concentrations of 125 and 62.5 µg mL−1, for DOPA‐Phe‐NH2 and DOPA‐Phe(4F)‐NH2, respectively. When the peptide assemblies are applied on a glass substrate by drop‐casting, they deactivate more than 99.9% of bacteriophage T4 and Canine coronavirus. Importantly, the peptide assemblies have low toxicity toward mammalian cells. Overall, the findings can provide a novel strategy for the design and development of antiviral coatings for a decreased risk of viral infections.
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