Viruses are natural supramolecular nanostructures that form spontaneously by molecular self-assembly of complex biomolecules. Peptide self-assembly is a versatile tool that allows mimicking viruses by creating their simplified versions through the design of functional, supramolecular materials with modularity, tunability, and responsiveness to chemical and physical stimuli. The main challenge in the design and fabrication of peptide materials is related to the precise control between the peptide sequence and its resulting supramolecular morphology. We provide an overview of existing sequence patterns employed for the development of spherical and fibrillar peptide assemblies that can act as viral mimetics, offering the opportunity to tackle the challenges of viral infections.

Ester hydrolysis is of wide biomedical interest, spanning from the green synthesis of pharmaceuticals to biomaterials' development. Existing peptide-based catalysts exhibit low catalytic efficiency compared to natural enzymes, due to the conformational heterogeneity of peptides. Moreover, there is lack of understanding of the correlation between the primary sequence and catalytic function. For this purpose, we statistically analyzed 22 EC 3.1 hydrolases with known catalytic triads, characterized by unique and well-defined mechanisms. The aim was to identify patterns at the sequence level that will better inform the creation of short peptides containing important information for catalysis, based on the catalytic triad, oxyanion holes and the triad residues microenvironments. Moreover, fragmentation schemes of the primary sequence of selected enzymes alongside the study of their amino acid frequencies, composition, and physicochemical properties are proposed. The results showed highly conserved catalytic sites with distinct positional patterns and chemical microenvironments that favor catalysis and revealed variations in catalytic site composition that could be useful for the design of minimalistic catalysts.

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With many industries discharging heavy metals into natural water resources, heavy metals have been found to accumulate in various living organisms which can ultimately threaten human life and pose a big threat to the environment. Thus, in the pursuit of a solution to the above mentioned problem, bioaccumulation has emerged as an interesting option for the removal of heavy metals from wastewater. In this paper, the effectiveness of the yeast Saccharomyces cerevisiae in the bioaccumulation of Cr3+ has been tested. Also, different factors influencing Cr3+ uptake have been discussed.  This work has demonstrated that Saccharomyces cerevisiae is an effective Cr3+ biosorbent for tannery wastewater. The conditions of use of this yeast to achieve optimal chromium (III) absorption are: i) when a growth of the biosorbent equivalent to a similar concentration of Cr3+ is obtained, which contains the residual water that needs to be treated; ii) the smaller the biosorbent is the better the biosorption; iii) the uptake of Cr3+ is more efficient when no extra growth medium is added to the wastewater; iv) the longer the exposure period of the yeast to Cr3+ , the bigger the Cr3+ reduction. Since Saccharomyces cerevisiae is an inexpensive, readily available source of biomass, this discovery could be of great use for a low-budget and efficient wastewater treatment system

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