A large number of glycoconjugates, built upon various scaffolds, have been widely employed as probes to study MLGI properties and also exploited as potential therapeutics. Some of these have exhibited potent anti-pathogenic infection properties. In most cases, their MLGI biophysical data were measured by conventional techniques, such as surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), and/or fluorescence competition assays. While ITC and SPR are widely used biophysical techniques which can provide quantitative binding affinity, thermodynamics, and/or kinetics data, they cannot provide key structural information, such as lectin binding site orientation, inter-binding site distance, and binding mode, which are very useful for designing potent, specific glycoconjugate inhibitors. Moreover, these methods can also suffer from limitations, such as low sensitivity (requiring large sample amounts), and unreliable binding affinity measurement for very strong interactions (with equilibrium dissociation constants, Kds, of low nM or below) for ITC, while the affinities measured by SPR can be strongly affected by the density and orientation of the immobilised binding partners. Furthermore, most previous MLGI studies have been based on the "passive" scaffolds, where nanomaterials are used as scaffolds only to create a polyvalent display of glycans to enhance their MLGI affinity, specificity, and/or therapeutic potency. The unique size-dependent optical/electrical properties of nano-scaffolds, the cornerstones of many nanomaterials, have not been explored as readouts for probing MLGI biophysical and structural data.