In addition, temporary trans-catheter SVAD Impella support has been advantageous for stabilization of decompensated 2V-RV patients or as bridge to durable SVAD support. Improved awareness of and access to specialist ACHD-HF teams offering mechanical support (and transplantation) for 2V-RV patients is increasingly urgent for this aging population, and will improve options and outcomes for these patients as HF emerges.The number of Fontan patients with circulatory failure and systolic dysfunction is growing rapidly. The last decade has demonstrated that ventricular assist device (VAD) is an effective therapy in properly selected patients. Herein, we discuss the current approach to patient selection, implantation, and patient management.With the substantial growth of pediatric ventricular assist device (VAD) support, there has been an expansion of the target population towards more complex patients, including congenital heart disease (CHD) with single ventricle (SV) physiology. The outcomes of Stage I and Stage II SV-CHD patients on VAD support from the Pedimacs database are poor, with less than 50% survival on VAD by the 3-month mark in both. The primary objective of this article is to describe the current state of VAD support for the failing Stage I and II SV-CHD circulation, to provide insight into potential areas of outcome improvement. We reviewed the published literature in the form of database and registry reports as well as single-center studies to discuss the outcomes of Stage I and Stage II SV-CHD patients on VAD support. Registry-based studies suggest that VAD support for the failing Stage I and Stage II SV-CHD circulations is challenging. However, the more promising outcomes in several single-institutional reports for both Stage I and Stage II SV-VAD indicate that the grim picture from the databases does not reflect the best outcomes that are possible to be achieved, potentially at experienced centers with higher volumes. Areas of future study and potential improvement including timely initiation of VAD support in the cohort of patients expected to not be a candidate for standard SV palliations, pump selection and the benefits of continuous-flow devices, and the decision-making for setting up the optimum circulation for VAD support, be it Fontan completion if feasible or takedown to shunt physiology.Although various phase transfer techniques have been used to make hydrophobic nanoparticles (NPs) water-soluble. However, these techniques have been limited by inefficient surface modification strategy that often stable NPs in aqueous solutions. Herein, we report the use of 3-aminophenylboronic acid (3-APBA) as a hydrophilic ligand for phase transfer of oleylamine (OA) capped Au NPs (OA@Au NPs) from non-hydrolytic system into aqueous solutions. The 3-APBA capped Au NPs (3-APBA@Au NPs) was mainly characterized using different analytical techniques to substantiate the efficiency of the phase transfer procedure. In this simple procedure, 3-APBA molecule was simultaneously used as both phase transfer and targeting ligand for bacteria recognition in one step. In principle, while free electron pair of amin (NH2) group of 3-APBAbind to surface of hydrophobic Au NPs for phase transfer, diol group can bind to glycan on the membrane of Staphylococcus aureus and Methicillin-resistant Staphylococcus aureus (MRSA) through proper cis-diol configuration. In addition, the resulting 3-APBA@Au NP can effectively catalyze the reduction of 4-nitrophenol (4-NP) to 4-aminophenol (4-AP) in the presence of sodium borohydride (NaBH4) in aqueous solution.Functionalizing C-H bond poses one of the most significant challenges for chemists providing them with very few substrate-specific synthetic routes. Despite being incredibly plastic in their enzymatic ability, they are confined with deficient enzymatic action and limited explicitness of the substrates. In this study, we have endeavored to characterize novel cytochrome P450 from Bacillus aryabhattai (CYP-BA), a homolog of CYP P450-BM3, by taking interdisciplinary approaches. We conducted structure and sequence comparison to understand the conservation pattern for active site residues, conserved fold, evolutionary relationships among others. Molecular dynamics simulations were performed to understand the dynamic nature and interaction with the substrates. Amcenestrant CYP-BA was successfully cloned, purified, and characterized. The enzyme's stability toward various physicochemical parameters was evaluated by UV-vis spectroscopy and Circular Dichroism (CD) spectroscopy. Various saturated fatty acids being the natural cytochrome P450 substrates were evaluated as catalytic efficiency of substrate oxidation by CYP-BA. The binding affinity of these natural substrates was monitored against CYP-BA by isothermal titration calorimetry (ITC). The catalytic performance of CYP-BA was satisfactory enough to proceed to the next step, that is, engineering to expand the substrate range to include polycyclic aromatic hydrocarbons (PAH). This is the first evidence of cloning, purifying and characterizing a novel homolog of CYP-BM3 to enable a better understanding of this novel biocatalyst and to provide a platform toward expanding its catalytic process through enzyme engineering.The development of a lignin peroxidase (LiP) that is thermostable even under acidic pH conditions is a main issue for efficient enzymatic lignin degradation due to reduced repolymerization of free phenolic products at acidic pH ( less then 3). Native LiP under mild conditions (half-life (t1/2) of 8.2 days at pH 6) exhibits a marked decline in thermostability under acidic conditions (t1/2 of only 14 min at pH 2.5). Thus, improving the thermostability of LiP in acidic environments is required for effective lignin depolymerization in practical applications. Here, we show the improved thermostability of a synthetic LiPH8 variant (S49C/A67C/H239E, PDB 6ISS) capable of strengthening the helix-loop interactions under acidic conditions. This variant retained excellent thermostability at pH 2.5 with a 10-fold increase in t1/2 (2.52 h at 25 °C) compared with that of the native enzyme. X-ray crystallography analysis showed that the recombinant LiPH8 variant is the only unique lignin peroxidase containing five disulfide bridges, and the helix-loop interactions of the synthetic disulfide bridge and ionic salt bridge in its structure are responsible for stabilizing the Ca2+-binding region and heme environment, resulting in an increase in overall structural resistance against acidic conditions.