An overview on the prevalence and potential impact of antimicrobials and antimicrobial resistance in the aquatic environment of India.

India at present is one of the leading countries in antimicrobial drug production and use, leading to increasing antimicrobial resistance (AMR) and public health problems. Attention has mainly been focused on the human and food animals' contribution to AMR neglecting the potential contribution of the perceptibly degraded aquatic environment in India. The paper reviews the available published literature in India on the prevalence of antimicrobial residues and their dissemination pathways in wastewater of pharmaceutical industries, sewage treatment plants, hospitals, riverine, community pond water, and groundwater. The prevalence of antimicrobial residue concentration, pathogenic and non-pathogenic bacteria antimicrobial resistant bacteria (ARB), their drug resistance levels, and their specific antimicrobial resistant genes (ARGs) occurring in various water matrices of India have been comprehensively depicted from existing literature. The concentration of some widely used antimicrobials recorded from the sewage treatment plants and hospital wastewater and rivers in India has been compared with other countries. The ecotoxicological risk posed by these antimicrobials in the various water matrices in India indicated high hazard quotient (HQ) values for pharmaceutical effluents, hospital effluents, and river water. The degraded aquatic environment exhibited the selection of a wide array of co-existent resistant genes for antibiotics and metals. The review revealed improper use of antibiotics and inadequate wastewater treatment as major drivers of AMR contaminating water bodies in India and suggestion for containing the challenges posed by AMR in India has been proposed.

Ameliorative Potential of Rosuvastatin on Doxorubicin-induced Cardiotoxicity by Modulating Oxidative Damage in Rats

Objectives: The study aimed to explore the in vivo protective potential of rosuvastatin (ROSS), an oral antihyperlipidemic drug against doxorubicin (DOXO) induced cardio toxicity in rats. Materials and Methods: Cardiac toxicity was induced by DOXO injection (10 mg/kg, i.p.), once on the 20th day of the experiment. Except for the control rats, all were received DOXO and the study was continued for up to 21 days. The influence of ROSS on acute treatment was analyzed by quantification of cardiac marker enzymes such as creatine kinase-MB (CK-MB), lactate dehydrogenase (LDH) and liver marker enzymes like aspartate aminotransferase (AST), alanine aminotransferase (ALT) along with the measurement of in vivo antioxidants like superoxide dismutase and catalase. To observe histological changes of myocardial tissue hematoxylin and eosin staining were used. Results: Acute administration of DOXO resulted in a marked rise of cardiac marker enzymes that confirms the myocardial damage compared to control animals whereas administration of ROSS (10 mg/kg, p.o.) resulted in the significant reduction of CK-MB, LDH levels (p<0.05) and AST, ALT levels to a remarkable extent. Moreover, ROSS administration significantly increased the activities of various in vivo antioxidant levels. Conclusion: From the results, the acute administration of ROSS showed significant cardioprotective property, which was evidenced by a significant reduction of cardiac and liver marker enzymes along with significant improvement of in vivo antioxidant activities. Furthermore the results were supported with histopathological observations. Hence, it can be concluded that cardioprotective potential of ROSS may be through attenuation of oxidative stress by modulating oxidative damage in rats.

Small-Molecule Probe for Sensing Serum Albumin with Consequential Self-Assembly as a Fluorescent Organic Nanoparticle for Bioimaging and Drug-Delivery Applications.

The recognition of a specific protein in blood serum amidst similar proteins is a challenging and vital endeavor in clinical diagnostics. Herein, we have described a small-molecule probe (DFPAC-OH) that can induce self-assembly of human serum albumin (HSA) and bovine serum albumin (BSA) to generate a highly sustainable fluorescent organic nanoparticle (NP), useful for imaging and in vitro drug-delivery applications. In the midst of similar proteins, DFPAC-OH selectively binds in a noncovalent manner to serum albumin. The specific binding tailors the fluorescence properties of DFPAC-OH. The lowest detection limit for BSA is 47 nM with a binding constant of 1.03 × 105 M-1. The probe can efficiently detect HSA in an artificial urine sample. Furthermore, the subsequent bovine albumin self-assembled nanoparticle (DFPAC-OH@BSA-NPs) displays a strong emission at 580 nm both in solution and in solid state. The nanoparticle is highly stable over a long pH range, covering the physiologic pH, and shows an excellent bioavailability to be used for sustainable cell imaging and drug-delivery applications. In addition, the cellular internalization and the pH-responsive drug-release behavior of a hydrophobic drug thymoquinone (TQ) encapsulated in DFPAC-OH@BSA-NPs (TQ-DFPAC-OH@BSA-NPs) have also been evaluated in A549 cell lines. The cytotoxic effect and quantification of intracellular reactive oxygen species (ROS) generation were further examined carefully to observe the anticancer property of TQ-DFPAC-OH@BSA-NPs. Therefore, the present system can simultaneously deliver drug molecules and image the event of delivery. The entire nanoparticles are characterized by transmission electron microscopy (TEM), scanning electron microscopy (SEM), dynamic light scattering (DLS), and infrared (IR) spectroscopy. The specific binding of DFPAC-OH is well supported by the molecular docking study, fluorescence lifetime measurement, and circular dichroism analysis.

Selective detection and bio-imaging of Pd2+ with novel 'C-CN' bond cleavage of cyano-rhodamine, cyanation with diaminomaleonitrile.

A new rhodamine based chemosensor, cyano-rhodamine, has been designed and synthesized with a green approach which shows a specific 'C-CN' bond breaking with the action of the Pd(2+) ion to produce the specific color and fluorescence of rhodamine 6G itself in solution and in HeLa cells.

Lens proteome map and alpha-crystallin profile of the catfish Rita rita.

Crystallins are a diverse group of proteins that constitute nearly 90% of the total soluble proteins of the vertebrate eye lens and these tightly packed crystallins are responsible for transparency of the lens. These proteins have been studied in different model and non-model species for understanding the modifications they undergo with ageing that lead to cataract, a disease of protein aggregation. In the present investigation, we studied the lens crystallin profile of the tropical freshwater catfish Rita rita. Profiles of lens crystallins were analyzed and crystallin proteome maps of Rita rita were generated for the first time. alphaA-crystallins, member of the alpha-crystallin family, which are molecular chaperons and play crucial role in maintaining lens transparency were identified by 1- and 2-D immunoblot analysis with anti-alphaA-crystallin antibody. Two protein bands of 19-20 kDa were identified as alphaA-crystallins on 1-D immunoblots and these bands separated into 10 discrete spots on 2-D immunoblot. However, anti-alphaB-crystallin and antiphospho-alphaB-crystallin antibodies were not able to detect any immunoreactive bands on 1- and 2-D immunoblots, indicating alphaB-crystallin was either absent or present in extremely low concentration in Rita rita lens. Thus, Rita rita alpha-crystallins are more like that of the catfish Clarias batrachus and the mammal kangaroo in its alphaA- and alphaB-crystallin content (contain low amount from 5-9% of alphaB-crystallin) and unlike the dogfish, zebrafish, human, bovine and mouse alpha-crystallins (contain higher amount of alphaB-crystallin from 25% in mouse and bovine to 85% in dogfish). Results of the present study can be the baseline information for stimulating further investigation on Rita rita lens crystallins for comparative lens proteomics. Comparing and contrasting the alpha-crystallins of the dogfish and Rita rita may provide valuable information on the functional attributes of alphaA- and alphaB-isoforms, as they are at the two extremes in terms of alphaA-and alphaB-crystallin content.