Effective role of tannic acid in the fabrication of hydrophobic, oleophilic, antibacterial, boron nitride/chlorobutyl rubber nanocomposite for reusable protective clothing and oil-water separation.

Boron Nitride (h-BN) possesses unique qualities like increased thermal conductivity, non-toxic nature, and environmental friendliness; hence, it is a good reinforcing agent for chlorobutyl rubber (CIIR). Tannic acid (TA) holds excellent bio-functional properties and is considered as an exceptional bio-exfoliating agent. Hence, in this study, we have utilized the bio-exfoliating ability of TA to exfoliate h-BN and evaluate its efficiency in reinforcing the CIIR matrix.

Mutational scan inferred binding energetics and structure in intrinsically disordered protein CcdA.

Unlike globular proteins, mutational effects on the function of Intrinsically Disordered Proteins (IDPs) are not well-studied. Deep Mutational Scanning of a yeast surface displayed mutant library yields insights into sequence-function relationships in the CcdA IDP. The approach enables facile prediction of interface residues and local structural signatures of the bound conformation.

Ter-Seq: A high-throughput method to stabilize transient ternary complexes and measure associated kinetics.

Regulation of biological processes by proteins often involves the formation of transient, multimeric complexes whose characterization is mechanistically important but challenging. The bacterial toxin CcdB binds and poisons DNA Gyrase. The corresponding antitoxin CcdA extracts CcdB from its complex with Gyrase through the formation of a transient ternary complex, thus rejuvenating Gyrase.

Combining cysteine scanning with chemical labeling to map protein-protein interactions and infer bound structure in an intrinsically disordered region.

The genome harbours nine toxin-antitoxin (TA) systems of the mazEF family. These consist of two proteins, a toxin and an antitoxin, encoded in an operon. While the toxin has a conserved fold, the antitoxins are structurally diverse and the toxin binding region is typically intrinsically disordered before binding.

The High Mutational Sensitivity of ccdA Antitoxin Is Linked to Codon Optimality.

Deep mutational scanning studies suggest that synonymous mutations are typically silent and that most exposed, nonactive-site residues are tolerant to mutations. Here, we show that the ccdA antitoxin component of the Escherichia coli ccdAB toxin-antitoxin system is unusually sensitive to mutations when studied in the operonic context. A large fraction (∼80%) of single-codon mutations, including many synonymous mutations in the ccdA gene shows inactive phenotype, but they retain native-like binding affinity towards cognate toxin, CcdB.

Ligand-protected nanoclusters and their role in agriculture, sensing and allied applications.

Nano biotechnology, when coupled with green chemistry, can revolutionize human life because of the vast opportunities and benefits it can offer to the quality of human life. Luminescent metal nanoclusters (NCs) have recently developed as a potential research area with applications in different areas like medical, imaging, sensing etc. Recently these new candidates have proved to be beneficial in the food supply chain enabling controlled release of nutrients, pesticides and as nanosensors for the detection of contaminants and play roles in healthy food storage and maintaining food quality.

Reducing Vibrio load in Artemia nauplii using antimicrobial photodynamic therapy: a promising strategy to reduce antibiotic application in shrimp larviculture.

We propose antimicrobial photodynamic therapy (aPDT) as an alternative strategy to reduce the use of antibiotics in shrimp larviculture systems. The growth of a multiple antibiotic resistant Vibrio harveyi strain was effectively controlled by treating the cells with Rose Bengal and photosensitizing for 30 min using a halogen lamp. This resulted in the death of >50% of the cells within the first 10 min of exposure and the 50% reduction in the cell wall integrity after 30 min could be attributed to the destruction of outer membrane protein of V.