BACKGROUND Carbohydrate-protein interactions participate in many biological functions. To characterize the binding interactions represents a longstanding challenge. METHOD We developed a glycan membrane array to study the interactions of carbohydrates with lectins, proteins and viruses, including 17 lectins, four antibodies (that are specific to different Lewis antigens), one recombinant H5N1 hemagglutinin, and five influenza B clinical isolates. RESULTS The results were found to be comparable to previous reports, indicating the efficacy and reliability of our developed method. CONCLUSION This carbohydrate membrane array represents a convenient, reliable and low-cost method to examine the carbohydrate-binding features of various proteins, high-throughput drug screening and the glycan-binding surveillance of influenza viruses.

This paper details the incorporation of a water-soluble deep cavitand into a membrane bilayer assembled onto a nanoglassified surface for study of molecular recognition in a membrane-mimicking setting. The cavitand retains its host properties, and real-time analysis of the host:guest properties of the membrane:cavitand complex via surface plasmon resonance and fluorescence microscopy is described. The host shows selectivity for choline-derived substrates, and no competitive incorporation of substrate is observed in the membrane bilayer. A variety of trimethylammonium-derived substrates are suitable guests, displaying varied binding affinities in a millimolar range. The membrane:cavitand:guest complexes can be subsequently used to capture NeutrAvidin protein at the membrane surface if a biotin-derived guest molecule is used. The surface coverage of NeutrAvidin is affected by the spacer used to derivatize the biotin. Increased distance from the bilayer allows a higher concentration of protein to be immobilized, suggesting a diminishing detrimental steric effect when the binding event is shifted away from the surface.

Optical biosensor technology continues to be the method of choice for label-free, real-time interaction analysis. But when it comes to improving the quality of the biosensor literature, education should be fundamental. Of the 1413 articles published in 2008, less than 30% would pass the requirements for high-school chemistry. To teach by example, we spotlight 10 papers that illustrate how to implement the technology properly. Then we grade every paper published in 2008 on a scale from A to F and outline what features make a biosensor article fabulous, middling or abysmal. To help improve the quality of published data, we focus on a few experimental, analysis and presentation mistakes that are alarmingly common. With the literature as a guide, we want to ensure that no user is left behind. Copyright (c) 2009 John Wiley & Sons, Ltd.

An electrochemical method that uses glucose labeled with an electroactive compound was developed to evaluate the binding of wheat germ agglutinin (WGA) to cellohexose-modified magnetic microbeads. Cellohexose was attached to amino groups on the magnetic bead surface via formation of a Schiff's base. The labeled glucose acts as an electrochemical probe to monitor binding events between WGA and the cellohexose-modified beads. For a known quantity of cellohexose-modified beads, binding of WGA with cellohexose-modified beads was evaluated based on changes in electrochemical response of the labeled glucose. In particular, the peak current decreased as the concentration of WGA increased. Furthermore, the binding affinities of WGA for beads modified with four different cello-oligosaccharides were systematically compared using a voltammetric method.

In this paper, we present a surface-plasmon-resonance-based immunosensor for the real-time detection of cortisol and cortisone levels in urine and saliva samples. The method proposed here is simple, rapid, economic, sensitive, robust, and reproducible thanks also to the special features of the polycarboxylate-hydrogel-based coatings used for the antibody immobilization. The sensor surface displays a high level of stability during repeated regeneration and affinity reaction cycles. The immunosensor shows high specificity for cortisol and cortisone; furthermore, no significant interferences from other steroids with a similar chemical structure have been observed. The suitability of the hydrogel coating for the prevention of nonspecific binding is also investigated. A good correlation is noticed between the results obtained by the proposed method and the reference liquid chromatography/tandem mass spectrometry method for the analysis of cortisol and cortisone in urine and saliva samples. Standard curves for the detection of cortisol and cortisone in saliva and urine are characterized by a detection limit less than 10 mug l(-1), sufficiently sensitive for both clinical and forensic use.