Iulia Arghir

Smart design of fiber optic surfaces for improved plasmonic biosensing

Although the phenomenon of surface plasmon resonance (SPR) is known for more than a century now, traditional prism-based SPR platforms have hardly escaped the research laboratories despite being recognized for the sensitive and specific performance. Significant efforts have been made over the last years to overcome their existing limitations by coupling the SPR phenomenon to the fiber optic (FO) technology. While this platform has been promoted as cost-effective and simpler alternative capable of handling label-free bioassays, quantification and real-time monitoring of biomolecular interactions, examples of its applicability in sensing and biosensing remain to date very limited. The FO-SPR system is still in development and requires further advancements for reaching the stability and sensitivity of the benchmark SPR systems. Among existing strategies for device improvement, those based on modifying the FO tips using nanomaterials are mostly studied. These small-scale objects provide a wide range of possibilities for alternating the architecture of the FO sensitive zone, enabling also unique effects such as localized SPR (LSPR). This mini-review summarizes the latest innovations in the fabrication procedures which use nanoparticles or other nanomaterials, aiming at FO-SPR technology performance improvements, as well as addition of new device features and functionalities.

Mechanism of Nonpolar Model Substances to Inhibit Primary Gushing Induced by Hydrophobin HFBI.

In this work, the interactions of a well-studied hydrophobin with different types of nonpolar model substances and their impact on primary gushing is evaluated. The nature, length, and degree of saturation of nonpolar molecules are key parameters defining the gushing ability or inhibition. When mixed with hydrophobins, the nonpolar molecule-hydrophobin assembly acts as a less gushing or no gushing system. This effect can be explained in the framework of a competition effect between non-polar systems and CO2 to interact with the hydrophobic patch of the hydrophobin. Interactions of these molecules with hydrophobins are promoted as a result of the similar size of the nonpolar molecules with the hydrophobic patch of the protein, at the expense of the formation of nanobubbles with CO2. In order to prove the presence of interactions and to unravel the mechanisms behind them, a complete set of experimental techniques was used. Surface sensitive techniques clearly show the presence of the interactions, whose nature is not covalent nor hydrogen bonding according to infrared spectroscopy results. Interactions were also reflected by particle size analysis in which mixtures of particles displayed larger size than their pure component counterparts. Upon mixing with nonpolar molecules, the gushing ability of the protein is significantly disrupted.