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Nanoparticles are key components underlying recent technological advances in various industrial and medical fields, and thus understanding their mode of interaction with biological systems is essential., Nanoparticles are key components underlying recent technological advances in various industrial and medical fields, and thus understanding their mode of interaction with biological systems is essential. However, while several nanoparticle systems have been shown to interact with blood platelets, many questions remain concerning the mechanisms of platelet activation and the role that the physicochemical properties of nanoparticles play in inducing platelet aggregation. Here, using negatively charged polystyrene nanoparticles with sizes of 25, 50, 119, 151, 201 nm and negatively charged platinum nanoparticles with sizes of 7 and 73 nm, we show that it is not the size of the nanoparticles but rather the nanoparticle surface area that is critical in mediating the effects on platelet activation. The nanoparticles stimulate platelet aggregation through passive (agglutination) and activation of integrin αIIbβ3 through a pathway regulated by Src and Syk tyrosine kinase.

The development of stimuli-responsive interfaces between synthetic materials and biological systems is providing the unprecedented ability to modulate biomolecular interactions for a diverse range of biotechnological and biomedical applications. Antibody–antigen binding interactions are at the heart of many biosensing platforms, but no attempts have been made yet to control antibody–antigen binding in an on-demand fashion. Herein, a molecular surface was designed and developed that utilizes an electric potential to drive a conformational change in surface bound peptide moiety, to give on-demand control over antigen–antibody interactions on sensor chips. The molecularly engineered surfaces allow for propagation of conformational changes from the molecular switching unit to a distal progesterone antigen, resulting in promotion (ON state) or inhibition (OFF state) of progesterone antibody binding. The approach presented here can be generally applicable to other antigen–antibody systems and meets the technological needs for in situ long-term assessment of biological processes and disease monitoring on-demand.

Gold surfaces were molecularly tailored with a saccharide binding motif capable of covalently adhering cells. This facilitated communication via the macrophage membrane with implications for understanding mammalian cell signalling., The fabrication of a molecularly tailored surface functionalised with a saccharide binding motif, a phenyl boronic acid derivative is reported. The functionalised surface facilitated the transfer of electrons, via unique electronic interactions mediated by the presence of the boronic acid, from a macrophage cell line. This is the first example of eukaryotic cellular-electrical communication mediated by the binding of cells via their cell–surface saccharide units.

A hierarchical bottom-up route exploiting reversible covalent interactions with boronic acids and so-called click chemistry for selective glycoprotein detection is described. The self-assembled and imprinted surfaces confer high binding affinities, nanomolar sensitivity, exceptional glycoprotein specificity and selectivity., Many glycoproteins are intimately linked to the onset and progression of numerous heritable or acquired diseases of humans, including cancer. Indeed the recognition of specific glycoproteins remains a significant challenge in analytical method and diagnostic development. Herein, a hierarchical bottom-up route exploiting reversible covalent interactions with boronic acids and so-called click chemistry for the fabrication of glycoprotein selective surfaces that surmount current antibody constraints is described. The self-assembled and imprinted surfaces, containing specific glycoprotein molecular recognition nanocavities, confer high binding affinities, nanomolar sensitivity, exceptional glycoprotein specificity and selectivity with as high as 30 fold selectivity for prostate specific antigen (PSA) over other glycoproteins. This synthetic, robust and highly selective recognition platform can be used in complex biological media and be recycled multiple times with no performance decrement.

Gold is a standard surface for attachment of thiol-based self-assembled monolayers (SAMs). To achieve uniform defect free SAM coatings, which are essential for bio/chemical sensing applications, the gold surface must have low roughness, and be highly orientated. These requirements are normally achieved by either heating during Au deposition or post deposition Au surface annealing. This paper shows that room temperature deposited gold, can afford equivalent gold surfaces, if the gold deposition parameters are carefully controlled. This observation is an important result as heating (or annealing) of the deposited gold can have a detrimental effect on the mechanical properties of the silicon on which the gold is deposited used in microsensors. The paper presents the investigation of the morphology and crystalline structure of Au film prepared by thermal evaporation at room temperature on silicon. The effect of gold deposition rate is studied, and it is shown that by increasing the deposition rate from 0.02 nm s-1 to 0.14 nm s-1 the gold surface RMS roughness decreases, whereas the grain size of the deposited gold is seen to follow a step function decreasing suddenly between 0.06 and 0.10 nm s-1. The XRD intensity of the preferentially [111] orientated gold crystallites is also seen to increase as the deposition rate increases up to a deposition rate of 0.14 nm s-1. Formation and characterization of 1-dodecanethiol on these Au coated samples is also studied using contact angle. It is shown that by increasing the Au deposition rate the contact angle hysteresis (CAH) decreases until it plateaus, for a deposition rate greater than 0.14 nm s-1, where the CAH is smaller than 9 degrees which is an indication of homogeneous SAM formation, on a smooth surface.

Our ability to tailor the electronic properties of surfaces by nanomodification is paramount for various applications, including development of sensing, fuel cell, and solar technologies. Moreover, in order to improve the rational design of conducting surfaces, an improved understanding of structure/function relationships of nanomodifications and effect they have on the underlying electronic properties is required. Herein, we report on the tuning and optimization of the electrochemical properties of indium tin oxide (ITO) functionalized with single-walled carbon nanotubes (SWCNTs). This was achieved by controlling in situ grafting of aryl amine diazonium films on the nanoscale which were used to covalently tether SWCNTs. The structure/function relationship of these nanomodifications on the electronic properties of ITO was elucidated via time-of-flight secondary ion mass spectrometry and electrochemical and physical characterization techniques which has led to new mechanistic insights into the in situ grafting of diazonium. We discovered that the connecting bond is a nitro group which is covalently linked to a carbon on the aryl amine. The increased understanding of the surface chemistry gained through these studies enabled us to fabricate surfaces with optimized electron transfer kinetics. The knowledge gained from these studies allows for the rational design and tuning of the electronic properties of ITO-based conducting surfaces important for development of various electronic applications.

Electrically switchable surfaces based on oligopeptides are ubiquitous in both switching specific protein interactions in highly fouling media while still offering the non-specific protein-resistance to the surface., Herein, electrically switchable mixed self-assembled monolayers based on oligopeptides have been developed and investigated for their suitability in achieving control over biomolecular interactions in the presence of complex biological conditions. Our model system, a biotinylated oligopeptide tethered to gold within a background of tri(ethylene glycol) undecanethiol, is ubiquitous in both switching specific protein interactions in highly fouling media while still offering the non-specific protein-resistance to the surface. Furthermore, the work demonstrated that the performance of the switching on the electro-switchable oligopeptide is sensitive to the characteristics of the media, and in particular, its protein concentration and buffer composition, and thus such aspects should be considered and addressed to assure maximum switching performance. This study lays the foundation for developing more realistic dynamic extracellular matrix models and is certainly applicable in a wide variety of biological and medical applications.