Investigating the Effectiveness of mqsR-Peptide Nucleic Acid as a Novel Solution for the Eradication of Persister Cells in Clinical Isolates of Escherichia coli.

Background: Bacterial persisters are non- or slow-growing phenotypic variants that may be responsible for recalcitrance and relapse of persistent infections and antibiotic failure. In Escherichia coli, mqsRA is a well-known type II toxin-antitoxin system associated with persister cell formation. This study aimed to investigate the efficiency of an antisense peptide nucleic acid (PNA) targeting mqsRA in eliminating E.

Selective Detection of Cancer Cells Using Magnetic Nanowires.

The main bottleneck for implementing magnetic nanowires (MNWs) in cell-biology research for multimodal therapeutics is the inapplicability of the current state of the art for selective detection and stimulation of MNWs. Here, we introduce a methodology for selective detection of MNWs in platforms that have multiple magnetic signals, such as future multimodal therapeutics. After characterizing the signatures of MNWs, MNWs were surface-functionalized and internalized into canine osteosarcoma (OSCA-8) cancer cells for cell labeling, manipulation, and separation.

Application of meta- and para-Phenylenediamine as Enhanced Oxime Ligation Catalysts for Protein Labeling, PEGylation, Immobilization, and Release.

Meta- and para-phenylenediamines have recently been shown to catalyze oxime and hydrazone ligation reactions at rates much faster than aniline, a commonly used catalyst. Here, we demonstrate how these new catalysts can be used in a generally applicable procedure for fluorescent labeling, PEGylation, immobilization, and release of aldehyde- and ketone- functionalized proteins. The chemical orthogonality of phenylenediamine-catalyzed oxime ligation versus copper-catalyzed click reaction has also been harnessed for simultaneous dual labeling of bifunctional proteins containing both aldehyde and alkyne groups in high yield.

Chemoenzymatic site-specific reversible immobilization and labeling of proteins from crude cellular extract without prior purification using oxime and hydrazine ligation.

In a facile and potentially general method for protein modification at the C-terminus, aldehyde-modified proteins, obtained from enzymatic protein prenylation, react rapidly with hydrazide and aminooxy surfaces and fluorophores at neutral pH and in micromolar concentration ranges of reagents. This strategy was used for fluorescent labeling of eGFP-CVIA, as a model protein, with aminooxy and hydrazide fluorophores or PEGs, and immobilization onto and subsequent release of the protein from hydrazide-functionalized agarose beads using hydrazone-oxime exchange. This method is described in detail here and provides site-specifically PEGylated or fluorescently labeled proteins starting from crude cellular extract in three steps: prenylation, capture, and release.

A highly efficient catalyst for oxime ligation and hydrazone-oxime exchange suitable for bioconjugation.

Imine-based reactions are useful for a wide range of bioconjugation applications. Although aniline is known to catalyze the oxime ligation reaction under physiological conditions, it suffers from slow reaction kinetics, specifically when a ketone is being used or when hydrazone-oxime exchange is performed. Here, we report on the discovery of a new catalyst that is up to 15 times more efficient than aniline.