Label-free determination of diffusion coefficients at the nanoscale through modelling of the Surface Plasmon Resonance signal.

Surface plasmon resonance (SPR) is normally used to measure the kinetic parameters of biomolecular interactions between a molecule immobilized on a gold surface and another one flowing in a microfluidic channel above the surface. During the SPR measurements, convection-diffusion phenomena occur inside the microfluidic channels, but they are generally minimized by appropriate experimental setup in order to obtain diffusion free kinetic parameters of the molecular interactions. In this work, for the first time, a commercial SPR apparatus has been used to obtain non canonical scientific parameters.

Mutations in the essential outer membrane protein BamA contribute to Escherichia coli resistance to the antimicrobial peptide TAT-RasGAP.

Antimicrobial peptides (AMPs) are promising alternatives to classical antibiotics against antibiotic-resistant pathogens. TAT-RasGAP is an AMP with broad range antibacterial activity, but its mechanism of action is unknown. In this study, we analyzed a strain of Escherichia coli with extensive resistance to TAT-RasGAP but not to other AMPs that we obtained after twenty passages during an in vitro resistance selection experiment.

A VEGF Fragment Encompassing Residues 10-30 Inhibits Aβ1-42 Amyloid Aggregation and Exhibits Neuroprotective Properties Matching the Full-Length Protein.

The intricate relationship between brain vascular diseases and neurodegeneration has garnered increased attention in the scientific community. With an aging population, the incidence of these two conditions is likely to increase, making it imperative to understand the underlying common molecular mechanisms and unveiling novel avenues for therapy. Prompted by the observation that Aβ peptide aggregation has been implicated in the development of cerebral amyloid angiopathy (CAA) and that elevated concentrations of vascular endothelial growth factor (VEGF) in the cerebrospinal fluid (CSF) have been correlated with less cognitive decline in Alzheimer's disease (AD), we demonstrate that a small peptide (Pep9) encompassing the 10-30 sequence of VEGF exhibits significant ability to inhibit the aggregation of the Aβ1-42 peptide, as well as the formation of toxic oligomers.