Luminescent lanthanide metallopeptides for biomolecule sensing and cellular imaging.

Lanthanide ions display unique luminescent properties that make them particularly attractive for the development of bioprobes, including long-lived excited states that allow the implementation of time-gated experiments and the elimination of background fluorescence associated with biological media, as well as narrow emission bands in comparison with typical organic fluorophores, which allow ratiometric and multiplex assays. These luminescent complexes can be combined with peptide ligands to endow them with additional targeting, responsiveness, and selectivity, thus multiplying the opportunities for creative probe design. In this feature article we will present some of the main strategies that researchers have used to develop lanthanide metallopeptide probes for the detection of proteins and nucleic acids, as well as for monitoring enzymatic activity and cellular imaging.

Luminescent Ln(III)-Metallopeptide Sensors for Monitoring Elastase B Activity in Complex Biological Media.

The detection and monitoring of and its virulence factors, such as the LasB protease, are crucial for managing bacterial infections. Traditional fluorescent sensors for this protease face limitations in bacterial cultures due to interference from pigments like pyoverdine secreted by this opportunistic pathogen. We report here a Ln(III)-metallopeptide that combines a DO3A-Ln(III) complex and a sensitizing unit via a short peptide sequence as a simple, tunable, and selective probe for detecting 's LasB.

Structure of graphene oxide-phospholipid monolayers: A grazing incidence X-ray diffraction and neutron and X-ray reflectivity study.

Hypothesis: Graphene oxide-based nanotechnology has aroused a great interest due to its applications in the biomedical and optoelectronic fields. The wide use of these materials makes it necessary to study its potential toxicity associated with the inhalation of Graphene Oxide (GO) nanoparticles and its interaction with the lung surfactant. Langmuir monolayers have proven to be an excellent tool for studying the properties of the lung surfactant and the effect of intercalation of nanoparticles on its structure and properties.

Site-Selective C-H Amination of Phenol-Containing Biomolecules.

A C-N bond-forming cross-dehydrogenative coupling of a collection of Tyr-containing peptides and estrogens with heteroarenes is described. This oxidative coupling is distinguished by its scalability, operational simplicity, and air tolerance and enables the appendance of phenothiazines and phenoxazines in phenol-like compounds. When incorporated into a Tb(III) metallopeptide, the Tyr-phenothiazine moiety acts as a sensitizer for the Tb(III) ion, providing a new tool for the design of luminescent probes.

Probing Tyrosine Nitration with a Small Tb -Metallopeptide.

Tyrosine nitration, a post-translational modification (PTM) that takes place under nitrosative stress conditions, occurs through a non-enzymatic peroxynitrite-mediated reaction. Although protein nitration has long been considered an irreversible PTM involved in nitrosative stress-associated diseases, it has also been suggested to be a regulatory mechanism of signal transduction. Therefore, the development of tools that help to understand this protein modification is of great interest.

Self-assembled peptide-inorganic nanoparticle superstructures: from component design to applications.

Peptides have become excellent platforms for the design of peptide-nanoparticle hybrid superstructures, owing to their self-assembly and binding/recognition capabilities. Morover, peptide sequences can be encoded and modified to finely tune the structure of the hybrid systems and pursue functionalities that hold promise in an array of high-end applications. This feature article summarizes the different methodologies that have been developed to obtain self-assembled peptide-inorganic nanoparticle hybrid architectures, and discusses how the proper encoding of the peptide sequences can be used for tailoring the architecture and/or functionality of the final systems.

The Transmembrane Protein Semi1 Positions Gamete Nuclei for Reciprocal Fertilization in Tetrahymena.

During sexual reproduction in the ciliate, Tetrahymena thermophila, cells of complementary mating type pair ("conjugate") undergo simultaneous meiosis and fertilize each other. In both mating partners only one of the four meiotic products is "selected" to escape autophagy, and this nucleus divides mitotically to produce two pronuclei. The migrating pronucleus of one cell translocates to the mating partner and fuses with its stationary pronucleus and vice versa.