Black phosphorus/silk fibroin films hamper filamentous and invasive growth of .

The ability of fungi and bacteria to form biofilms on surfaces poses a serious threat to health and a problem in industrial settings. In this work, we investigated how the surface stiffness of silk fibroin (SF) films is modulated by the interaction with black phosphorus (BP) flakes, quantifying the morphogenesis of cells. Raman and infrared (IR) spectroscopies, along with scanning transmission electron microscopy, allowed us to quantify the thickness and diameter of BP flakes dispersed in the SF matrix (, 5.

Hindered intermolecular stacking of anti-parallel telomeric G-quadruplexes.

Telomeric G-quadruplexes (G4s) are non-canonical DNA structures composed of TTAGGG repeats. They are extensively studied both as biomolecules key for genome stability and as promising building blocks and functional elements in synthetic biology and nanotechnology. This is why it is extremely important to understand how the interaction between G4s is affected by their topology.

Conformational transitions in redissolved silk fibroin films and application for printable self-powered multistate resistive memory biomaterials.

3D printing of water stable proteins with elastic properties offers a broad range of applications including self-powered biomedical devices driven by piezoelectric biomaterials. Here, we present a study on water-soluble silk fibroin (SF) films. These films were prepared by mixing degummed silk fibers and calcium chloride (CaCl) in formic acid, resulting in a silk I-like conformation, which was then converted into silk II by redissolving in phosphate buffer (PBS).

Molecular mechanisms behind BRACO19 and human telomeric G-quadruplex interaction.

Human telomeres (HTs) can form DNA G-quadruplex (G4), an attractive target for anticancer and antiviral drugs. HT-G4s exhibit inherent structural polymorphism, posing challenges for understanding their specific recognition by ligands. Here, we aim to explore the impact of different topologies within a small segment of the HT (Tel22) on its interaction with BRACO19, a rationally designed G4 ligand with high quadruplex affinity, already employed in in-vivo treatments.

Dynamic Personality of Proteins and Effect of the Molecular Environment.

Protein dynamics display distinct traits that are linked to their specific biological function. However, the interplay between intrinsic dynamics and the molecular environment on protein stability remains poorly understood. In this study, we investigate, by incoherent neutron scattering, the subnanosecond time scale dynamics of three model proteins: the mesophilic lysozyme, the thermophilic thermolysin, and the intrinsically disordered β-casein.