In recent years, nanotechnology has achieved a remarkable status in shaping the future of biological applications, especially in combating fungal diseases. Owing to excellence in nanotechnology, iron nanoparticles (Fe NPs) have gained enormous attention in recent years. In this review, we have provided a comprehensive overview of Fe NPs covering key synthesis approaches and underlying working principles, the factors that influence their properties, essential characterization techniques, and the optimization of their antifungal potential. In addition, the diverse kinds of Fe NP delivery platforms that command highly effective release, with fewer toxic effects on patients, are of great significance in the medical field. The issues of biocompatibility, toxicity profiles, and applications of optimized Fe NPs in the field of biomedicine have also been described because these are the most significant factors determining their inclusion in clinical use. Besides this, the difficulties and regulations that exist in the transition from laboratory to experimental clinical studies (toxicity, specific standards, and safety concerns) of Fe NPs-based antifungal agents have been also summarized.

Background: Arcobacter bivalviorum is an emerging foodborne pathogen particularly found in shellfish and other bivalves. This bacterium's metabolic versatility is highlighted by its possession of both the Pyruvate Dehydrogenase Complex (PDC) and Pyruvate:Ferredoxin Oxidoreductase (PFOR). The PFOR enzyme is crucial for linking glycolysis to the citric acid cycle. Previous studies of PFOR enzyme reveal its susceptibility to oxygen damage due to its reliance on Fe-S clusters for electron transfer.Methods: The current study employs bioinformatic approaches to explore the oxygen sensitivity of A. bivalviorum's PFOR, comparing it with Desulfovibrio africanus and Moorella thermoacetica. The UniProt database was used to obtain the sequences of PFOR from D. africanus (CAA70873), A. bivalviorum (AXH11209), and M. thermoacetica (Q2RMD6). This comparative analysis sheds light on the structural similarities and differences between the enzymes, providing a deeper understanding of their functional mechanisms.Result: PFOR enzyme is a heterodimer, with its functional subunits containing three [4Fe-4S]²⁺ clusters. Its exposed Fe-S clusters are vulnerable to oxygen and ROS, leading to enzyme inactivation. A comparison of PFOR sequences from D. africanus, M. thermoacetica, and A. bivalviorum reveals a crucial difference: the final 43 residues at the C-terminal of D. africanus are missing in the other two enzymes, depriving the M. thermoacetica and A. bivalviorum enzymes of a self-protective mechanism.Conclusion: Pyruvate:ferredoxin oxidoreductase (PFOR) in A. bivalviorum lacks protection from oxidative damage due to the absence of the final 43 amino acids at the C-terminal.Keywords: PFOR; Homology modeling; oxygen sensitivity; Foodborne pathogen

This research investigated the unstudied impact, in 416 cases of stone-induced hydronephrosis detected radiographically in 369 patients, of stone size on the stone’s location in the urinary tract and on the hydronephrosis grade. Most (62.5%) of the hydronephrosis cases were Grade 2; 17.1%, Grade 3; 10.6%, Grade 4; and 9.9%, Grade 1. The mean size of the stones reported in the renal pelvis, pelviureteric junction (PUJ), upper ureter (UU), midureter (MU), lower ureter (LU), and vesicoureteral junction (VUJ) that caused hydronephrosis were 23.03 ± 8.97 mm, 15.56 ± 6.59 mm, 12.91 ± 6.02 mm, 11.05 ± 4.27 mm, 10.41 ± 4.80 mm, and 6.73 ± 3.28 mm, respectively. The mean size of Grade 1-causing stones was 16.63 mm; Grade 2, 11.49 mm; Grade 3, 15.69 mm; and Grade 4, 21.23 mm. The mean stone size significantly decreased from the renal pelvis, through the PUJ, UU, MU, and LU, and down to the VUJ and increased as the hydronephrosis grade increased from Grade 2 to Grade 4. In conclusion, large-size stones were predominantly located in the renal pelvis and PUJ, with few located in the lower ureter, and no large stones reached the VUJ. Small-size stones were mostly located in the VUJ, with only one stone in the PUJ, and no small-size stones were present in the renal pelvis. Large-size stones caused severe hydronephrosis, and small-size stones caused grade 2 hydronephrosis. Increases in stone size decreased its passage rate in the ureter and increased the chance of causing high-grade hydronephrosis. These results alert urologists to adopt faster therapeutic procedures for larger stone sizes to reduce renal damage caused by obstructive uropathy.

Arcobacter spp., such as Arcobacter bivalviorum (A. bivalviorum), are free-living organisms found in diverse environments and associated with animals. They are considered emerging enteropathogens and potential zoonotic agents. Ribonucleotide reductase (RNR) is the key enzyme that is used to convert ribonucleotides into deoxyribonucleoside triphosphates (dNTPs). This process utilises radical-based chemistry and is crucial for DNA biosynthesis and repair. There are three RNR classes, with class I RNR the most studied, present in A. bivalviorum, eukaryotes, and many prokaryotes. Class I RNRs are further divided into three subclasses: Ia, Ib, and Ic. Class Ib RNRs use a dimanganese-oxo centre, unlike class Ia RNRs, which use a diiron-oxo centre. A. bivalviorum possesses a class Ia enzyme that requires a diferric tyrosyl radical cofactor located within its beta (β) subunit. Indeed, both the efficiency and fidelity of DNA synthesis are influenced by the stability of the tyrosyl radical (Y•) in the RNR, which is a critical aspect of its enzymatic function. This study investigates the stability of the Y-radical (Y•) site within the RNR β subunit of A. bivalviorum and the nature of the neighbouring amino acid residues. To achieve these goals, we developed a model of the RNR β subunit of A. bivalviorum, using the RNR β subunit of Aquifex aeolicus as a reference template (7aik.1. A PDB). The results provide some important details about the radical site and its surrounding residues, highlighting the influence of the protein structure on the stability of the radical. These findings may guide the development of novel inhibitors targeting this enzyme in A. bivalviorum.