Journal articles

Knowledge is now recognised as a prime driver of innovation, productivity and economic growth. The new economies will require heavy investment into research and development, education and training and the development of novel flows and relationships among the key players, government, academia and industry. The higher education sector will play a key role in furnishing the novel ideas and skilled personnel to enable this transition, but will require organisational and cultural change to be effective.

The reversible phosphorylation of proteins regulates many biological processes. Despite the technological advances in the enrichment and detection of phosphorylated proteins, the currently available techniques still struggle with the complexity of the human proteome. The aim of this review is to highlight the molecular recognition elements of the interaction between phosphorylated proteins and peptides and pTyr or pSer/Thr-binding domains.

Affinity chromatography is ideally suited to the purification of pharmaceutical proteins due to its unique bio-specificity characteristics. Tailor-made affinity ligands that represent a promising class of synthetic affinity ligands have been developed to target specific proteins and designed to mimic peptidal templates, natural biological recognition motifs, or complementary surface-exposed residues. These biomimetic ligands have been generated by a combination of rational design, combinatorial library synthesis, and subsequent screening of potential leads against target proteins.

Affinity chromatography represents a promising technique for decoding the proteomics universe. While conventional affinity purification is being used in conjunction with two-dimensional electrophoresis (2D-PAGE) and mass spectrometry (MS) for the study of proteomes and subproteomes, scientists are still confronted with the need for specific and tailor-made affinity ligands to target desired groups and families of proteins.

A novel toroidal coil geometry able to induce remote acoustic waves in quartz crystals has been evaluated for the development of (bio)sensors. Remote acoustic generation in air was obtained for two alternative toroidal coils, with corresponding electrical impedance changes of 40 Ω for a PDMS- and 140 Ω for a ferrite-supported toroid respectively.

Analyte-responsive holograms comprise a holographic grating embedded in a smart hydrogel film. The grating acts as a reporter that enables analyte induced changes in the thickness of the associated polymer film to be accurately determined. Interaction of these materials with a specific analyte or stimuli leads to a change in the colour, image or brightness of the hologram and these changes can be visualised directly or quantified using a simple colour reader.

The protein surface is the interface through which a protein molecule senses the external world. The composition of this interface, in charged, polar and/or hydrophobic residues is crucial for both the activity and stability of the protein. Protein immobilization on surfaces has been extensively explored as one of the most effective approaches for stabilization. The mechanism of stabilization, however, is still poorly understood, and usually the success of any method is more a matter of trial and error rather than the result of rational concepts.

A unique sensing platform, comprising an electromagnetic field detector and an acoustic resonator, has been used as a wireless system for remote sensing of biorecognition events. The MARS (Magnetic Acoustic Resonator Sensor) technique has proven useful for detecting the formation of protein multilayers derived from specific binding phenomena. The technique enables multifrequency analysis, without the need of electrodes attached to the sensing element, and also facilitates the in situ surface modification of the substrate for antibody attachment.

Firefly luciferase catalyses a two-step reaction, using ATP-Mg 2+, firefly luciferin and molecular oxygen as substrates, leading to the efficient emission of yellow-green light. We report the identification of novel luciferase mutants which combine improved pH-tolerance and thermostability and that retain the specific activity of the wild-type enzyme. These were identified by the mutagenesis of solvent-exposed non-conserved hydrophobic amino acids to hydrophilic residues in Photinus pyralis firefly luciferase followed by in vivo activity screening.

Measurement of blood L-lactate is used to assess and monitor exercise performance in sports medicine. This report describes the initial development of a holographic sensor, which employs a synthetic receptor, to enable the selective and continuous real-time measurement of L-lactate for eventual in vivo application. Three boronic acid-based receptors have been synthesized, integrated into thin acrylamide hydrogel films, and then subsequently transformed into holographic sensors.