Expression of concern: Comparison of photo- and Cu(I)-catalyzed "click" chemistries for the formation of carbohydrate SPR interfaces.

Expression of concern for 'Comparison of photo- and Cu(I)-catalyzed "click" chemistries for the formation of carbohydrate SPR interfaces' by Nazek Maalouli , , 2013, , 805-812, https://doi.org/10.1039/C2AN36272D.

Recent advances in the development of graphene-based surface plasmon resonance (SPR) interfaces.

Surface plasmon resonance (SPR) is a powerful technique for measurement of biomolecular interactions in real-time in a label-free environment. One of the most common techniques for plasmon excitation is the Kretschmann configuration, and numerous studies of ligand-analyte interactions have been performed on surfaces functionalized with a variety of biomolecules, for example DNA, RNA, glycans, proteins, and peptides. A significant limitation of SPR is that the substrate must be a thin metal film.

Comparison of photo- and Cu(I)-catalyzed "click" chemistries for the formation of carbohydrate SPR interfaces.

Understanding interactions of glycans with proteins in key biological events has seen the development of various analytical methods such as microarray techniques. Label-free approaches, such as surface plasmon resonance (SPR) techniques are particularly attractive and we explore here the potential of a novel interface composed of lamellar Ti/Au/silicon dioxide derivatized with sugars to probe lectin-sugar interactions by SPR. Two parallel surface functionalization strategies have been developed: one in which azide-functionalized surfaces are linked via a Cu(I) "click" method to alkynyl-derivatized glycan partners and another wherein perfluorophenyl azide-functionalized surfaces are reacted through a C-H insertion photocoupling reaction with underivatized glycans.

Development of a metal-chelated plasmonic interface for the linking of His-peptides with a droplet-based surface plasmon resonance read-off scheme.

Monolayers of metal complexes were covalently attached to the surface of lamellar SPR interfaces (Ti/Ag/a-Si(0.63)C(0.37)) for binding histidine-tagged peptides with a controlled molecular orientation.