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Carbamazepine is considered as an emerging pollutant since in aquatic environments is toxic for fish and difficult to degrade. The goal of this study was to isolate yeasts capable of degrading carbamazepine. A hospital wastewater sample was used as an inoculant to carry out three successive transfers in minimal mineral medium added with 50 mg L−1 of carbamazepine. The isolates were characterized by colonial and microscopic morphology. A yeast was identified by sequencing its ITS1-5.8S-ITS2 intergenic region and by constructing of a phylogenetic tree. A kinetics of carbamazepine degradation was done with an initial concentration of 150 mg L−1 and the residual drug was determined by HPLC-UV. A total of 12 isolates were obtained, one of them had the characteristics of yeast (Carba14), the others were bacteria. Yeast isolate Carba 14 grew at all concentrations of carbamazepine tested (50, 100, 150 and 200 mg L−1) and grew better than bacterial isolates. This isolate degraded carbamazepine with an efficiency of 30% within 25 days. Yeast isolate Carba 14 was identified as Candida palmioleophila Carba 14. Our study shows for the first time the isolation of C. palmioleophila Carba 14 with potential to degrade carbamazepine. [ABSTRACT FROM AUTHOR]

Background: The deterioration of the skin accentuates over time, affecting its aesthetic appearance. This is characterized by the weakening of the mechanisms involved in the regeneration and repair of the dermal matrix. Consequently, the skin losses elasticity and smoothness resulting in the formation of wrinkles. The alternatives for facial rejuvenation include surgery, injection of botulinum toxin, and the application of masks. Topic products are less invasive, can be self‐applied, and have an increased benefit/risk relationship. Aim: We developed a liquid formulation containing collagen hydrolyzed and evaluated the product by cutting‐edge technology in order to define proper its quality attributes. Methods: We employed nuclear magnetic resonance (NMR), size‐exclusion chromatography (SEC), and mass spectrometry (MS). Additionally, we analyzed its cosmetical effect in five volunteers and we demonstrate the product safety. Results: Our results demonstrate the following: (a) a stable secondary structure identity associated to the known triple helix arrangement in liquid and solid states; (b) a typical conformational flexibility depending on its hydration state; (c) thermal stability confirmed by liquid‐ and solid‐state nuclear magnetic resonance schemes; and (d) a molecular mass distribution of peptides between 0.5 and 19.5 kDa. The product faded wrinkles in the forehead, an effect that remained after removing the mask. The formula was non‐irritating and hypoallergenic. Conclusion: We characterized, using state‐of‐the‐art methodologies, the quality attributes that are critical for the safety and beneficial effect of a new collagen‐containing formula. [ABSTRACT FROM AUTHOR]

Neutralizing antibodies targeting the receptor-binding domain (RBD) of SARSCoV-2 are among the most promising strategies to prevent and/or treat COVID-19. However, as SARS-CoV-2 has evolved into new variants, most of the neutralizing antibodies authorized by the US FDA and/or EMA to treat COVID-19 have shown reduced efficacy or have failed to neutralize the variants of concern (VOCs), particularly B.1.1.529 (Omicron). Previously, we reported the discovery and characterization of antibodies with high affinity for SARS-CoV-2 RBD Wuhan (WT), B.1.617.2 (Delta), and B.1.1.529 (Omicron) strains. One of the antibodies, called IgG-A7, also blocked the interaction of human angiotensin-converting enzyme 2 (hACE2) with the RBDs of the three strains, suggesting it may be a broadly SARS-CoV-2 neutralizing antibody. Herein, we show that IgG-A7 efficiently neutralizes all three SARS-CoV-2 strains in plaque reduction neutralization tests (PRNTs). In addition, we demonstrate that IgG-A7 fully protects K18-hACE2 transgenic mice infected with SARS-CoV-2 WT. Our findings indicate that IgG-A7 could be a suitable candidate for developing antibody-based drugs to treat and/ or prevent SARS-CoV-2 VOCs infection. [ABSTRACT FROM AUTHOR]

We describe here the construction of a single domain antibody (sdAb) library consisting of grafting natural human HCDR3 fragments obtained from 200 healthy human donors into a synthetic framework region designed with the human germline IGHV3-23. After three rounds of panning against the hACE-2 receptor binding domain (RBD) of SARS-CoV-2, 90 clones were randomly picked and screened for binding to RBD and BSA. A total of 35 clones specifically bound RBD, with 9 clones showing unique sequences. Out of these unique clones, four blocked RBD:hACE2 interaction.. A Clone, termed sdC3, was expressed in E. coli and purified by Protein A, exhibiting the expected molecular mass of ≈18 kDa. Purified sdC3 had an affinity for RBD comparable to a potent neutralizing scFv and blocked the RBD:ACE2 interaction. Further, heat-treated sdC3 at 80 °C for 10 minutes retained its binding affinity, indicating high thermal stability, an advantageous property typical of sdAbs. Thus, the platform we developed for rapid isolation of fully human sdAbs set the stage for future discovery of diverse molecules with application not only in rapidly evolving viral diseases such as SARS-CoV-2 but also in other applications that require highly stable molecules. [ABSTRACT FROM AUTHOR]