Conducting polymer scaffolds combine the soft-porous structures of scaffolds with the electrical properties of conducting polymers. In most cases, such functional systems are developed by combining an insulating scaffold matrix with electrically conducting materials in a 3D hybrid network. However, issues arising from the poor electronic properties of such hybrid systems, hinder their application in many areas. This work reports on the design of a 3D electroactive scaffold, which is free of an insulating matrix. These 3D polymer constructs comprise of a water soluble conducting polymer (PEDOT:PSS) and multi-walled carbon nanotubes (MWCNTs). The insertion of the MWCNTs in the 3D polymer matrix directly contributes to the electron transport efficiency, resulting in a 7-fold decrease in resistivity values. The distribution of CNTs, as characterized by SEM and Raman spectroscopy, further define the micro- and nano-structural topography while providing active sites for protein attachment, thereby rendering the system suitable for biological/sensing applications. The resulting scaffolds, combine high porosity, mechanical stability and excellent conducting properties, thus can be suitable for a variety of applications ranging from tissue engineering and biomedical devices to (bio-) energy storage.
The detection of proteins is of central importance to biomolecular analysis and diagnostics. Typical immunosensing assays rely on surface-capture of target molecules, but this constraint can limit specificity, sensitivity, and the ability to obtain information beyond simple concentration measurements. Here we present a surface-free, single-molecule microfluidic sensing platform for direct digital protein biomarker detection in solution, termed digital immunosensor assay (DigitISA). DigitISA is based on microchip electrophoretic separation combined with single-molecule detection and enables absolute number/concentration quantification of proteins in a single, solution-phase step. Applying DigitISA to a range of targets including amyloid aggregates, exosomes, and biomolecular condensates, we demonstrate that the assay provides information beyond stoichiometric interactions, and enables characterization of immunochemistry, binding affinity, and protein biomarker abundance. Taken together, our results suggest a experimental paradigm for the sensing of protein biomarkers, which enables analyses of targets that are challenging to address using conventional immunosensing approaches.
The rapid emergence of drug-resistant bacteria and fungi poses a threat for healthcare worldwide. The development of novel effective small molecule therapeutic strategies in this space has remained challenging. Therefore, one orthogonal approach is to explore biomaterials with physical modes of action that have the potential to generate antimicrobial activity and, in some cases, even prevent antimicrobial resistance. Here, to this effect, we describe an approach for forming silk-based films that contain embedded selenium nanoparticles. We show that these materials exhibit both antibacterial and antifungal properties while crucially also remaining highly biocompatible and noncytotoxic toward mammalian cells. By incorporating the nanoparticles into silk films, the protein scaffold acts in a 2-fold manner; it protects the mammalian cells from the cytotoxic effects of the bare nanoparticles, while also providing a template for bacterial and fungal eradication. A range of hybrid inorganic/organic films were produced and an optimum concentration was found, which allowed for both high bacterial and fungal death while also exhibiting low mammalian cell cytotoxicity. Such films can thus pave the way for next-generation antimicrobial materials for applications such as wound healing and as agents against topical infections, with the added benefit that bacteria and fungi are unlikely to develop antimicrobial resistance to these hybrid materials.
Parkinson's disease (PD) is an increasingly prevalent and currently incurable neurodegenerative disorder linked to the accumulation of alpha-synuclein (alphaS) protein aggregates in the nervous system. While alphaS binding to membranes in its monomeric state is correlated to its physiological role, alphaS oligomerisation and subsequent aberrant interactions with lipid bilayers have emerged as key steps in PD-associated neurotoxicity. However, little is known of the mechanisms that govern the interactions of oligomeric alphaS (OalphaS) with lipid membranes and the factors that modulate such interactions. This is in large part due to experimental challenges underlying studies of OalphaS-membrane interactions due to their dynamic and transient nature. Here, we address this challenge by using a suite of microfluidics-based assays that enable in-solution quantification of OalphaS-membrane interactions. We find that OalphaS bind more strongly to highly curved, rather than flat, lipid membranes. By comparing the membrane-binding properties of OalphaS and monomeric alphaS (MalphaS), we further demonstrate that OalphaS bind to membranes with up to 150-fold higher affinity than their monomeric counterparts. Moreover, OalphaS compete with and displace bound MalphaS from the membrane surface, suggesting that disruption to the functional binding of MalphaS to membranes may provide an additional toxicity mechanism in PD. These findings present a unique binding mechanism of oligomers to model membranes, which can potentially be targeted to inhibit the progression of PD.
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