'Wild Type'.

In this opinion piece, we consider the meaning of the term 'wild type' in the context of microbiology. This is especially pertinent in the post-genomic era, where we have a greater awareness of species diversity than ever before. Genomic heterogeneity, evolution/selection pressures, definition of 'the wild', the size and importance of the pan-genome, gene-gene interactions (epistasis), and the nature of the 'wild-type gene' are all discussed.

Antiviral Activity of Peptide-Based Assemblies.

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.

Non-covalently embedded oxytocin in alkanethiol monolayer as Zn selective biosensor.

Peptides are commonly used as biosensors for analytes such as metal ions as they have natural binding preferences. In our previous peptide-based impedimetric metal ion biosensors, a monolayer of the peptide was anchored covalently to the electrode. Binding of metal ions resulted in a conformational change of the oxytocin peptide in the monolayer, which was measured using electrochemical impedance spectroscopy.

Structural preferences of an anti-fouling peptide: From single chain to small molecular assemblies.

The structural features of a tripeptide constituted by two different non-coded amino acids, 3,4-dihydroxy-L-phenylalanine (L-DOPA) and 4-fluoro-Phenylalanine, (Phe(4F)), have been investigated by means of classical mechanics simulations. This tripeptide had been characterised as an antifouling agent with great adhesion capabilities. In this work, its conformational preferences have been described in two different environments (gas phase and water solution), at three different pHs and with different degrees of terminal capping.

Amphiphilic Peptide with Dual Functionality Resists Biofouling.

Biofouling, the accumulation of organisms on surfaces, can lead to several undesirable phenomena, including hospital-acquired infections, blockage of water purification systems, and food contamination. The solution to the problem should be nontoxic and environmentally friendly, so that it could be applied on different surfaces and could come into contact with food, water, or human tissues. Peptides can provide such a solution, since they are biocompatible and biodegradable materials that can resist biofouling, either by preventing the attachment of organisms to the surface (antifouling) or by killing the bacteria (antimicrobial activity).

Expanding the Functional Scope of the Fmoc-Diphenylalanine Hydrogelator by Introducing a Rigidifying and Chemically Active Urea Backbone Modification.

Peptidomimetic low-molecular-weight hydrogelators, a class of peptide-like molecules with various backbone amide modifications, typically give rise to hydrogels of diverse properties and increased stability compared to peptide hydrogelators. Here, a new peptidomimetic low-molecular-weight hydrogelator is designed based on the well-studied -fluorenylmethoxycarbonyl diphenylalanine (Fmoc-FF) peptide by replacing the amide bond with a frequently employed amide bond surrogate, the urea moiety, aiming to increase hydrogen bonding capabilities. This designed ureidopeptide, termed Fmoc-Phe-NHCONH-Phe-OH (Fmoc-FuF), forms hydrogels with improved mechanical properties, as compared to those formed by the unmodified Fmoc-FF.

Preventing Biofilm Formation by Dairy-Associated Bacteria Using Peptide-Coated Surfaces.

Biofilm-forming bacteria, which colonize the surfaces of equipment in the dairy industry, may adversely affect the safety and quality of the milk and its products. Despite numerous efforts to combat biofilm formation, there is still no effective technological means to thoroughly solve the biofilm problem in the dairy industry. Here, we introduced peptide-based coating in order to modify the physical properties of the stainless steel surface by affecting its availability for bacterial adhesion.

Tailoring the self-assembly of a tripeptide for the formation of antimicrobial surfaces.

The accumulation of bacteria on surfaces is currently one of the greatest concerns for the management of proper healthcare systems, water and energy. Here, we describe the mechanism by which a single peptide forms two pH-dependent supramolecular particles that resist bacterial contamination. By using NMR and molecular dynamics (MD), we determined the structures of the peptide monomers and showed the forces directing the self-assembly of each structure under different conditions.

Rational Design of Amphiphilic Peptides and Its Effect on Antifouling Performance.

Biofouling, the unwanted adhesion of organisms to surfaces, has a negative impact on energy, food, water, and health resources. One possible strategy to fight biofouling is to modify the surface using a peptide-based coating that will change the surface properties. We reveal the importance of rational design and positioning of individual amino acids in an amphiphilic peptide sequence.

Electrochemical Approach for Effective Antifouling and Antimicrobial Surfaces.

Biofouling, the adsorption of organisms to a surface, is a major problem today in many areas of our lives. This includes: (i) health, as biofouling on medical device leads to hospital-acquired infections, (ii) water, since the accumulation of organisms on membranes and pipes in desalination systems harms the function of the system, and (iii) energy, due to the heavy load of the organic layer that accumulates on marine vessels and causes a larger consumption of fuel. This paper presents an effective electrochemical approach for generating antifouling and antimicrobial surfaces.

Bio-inspired antifouling approaches: the quest towards non-toxic and non-biocidal materials.

Biofouling is an undesirable process in which organisms and their by-products encrust a surface. Antifouling solutions are of great importance since biofouling has negative effects on numerous species, ecosystems, and areas including water treatment facilities, health-care systems, and marine devices. Many useful solutions have been developed in the last few decades.

Self-assembly of a tripeptide into a functional coating that resists fouling.

This communication describes the self-assembly of a tripeptide into a functional coating that resists biofouling. Using this peptide-based coating we were able to prevent protein adsorption and interrupt biofilm formation. This coating can be applied on numerous substrates and therefore can serve in applications related to health care, marine and water treatment.

Co-assembly of aromatic dipeptides into spherical structures that are similar in morphology to red and white blood cells.

This paper describes the co-assembly of two aromatic dipeptides, diphenylalanine and Fmoc-l-DOPA(acetonated)-d-Phe-OMe, into different spherical structures that are similar in morphology to either red or white blood cells. Under the examined experimental conditions, each of the peptides formed spherical nanostructures, but a mixture of the two peptides generated new types of assemblies. When the concentration of the two peptides was 1 mg mL they self-assembled into oval biconcave disk nanostructures that are similar in morphology to red blood cells.