We have demonstrated this sensing platform can quantify sialylation levels of intact glycoproteins (mixtures of fetuin and asialofetuin). In our quest for deeper insights, we evaluate the capability of this sensing platform for distinguish sialic acid linkages. Sialic acids could link with other glycan entities in multiple linkage forms (α2,3, α2,6, α2,8 or α2,9) , and the most common linkages for sialic acids to other glycans are α2,3 and α2,6 . It is crucial to differentiate sialic acids glycosidic linkages since the linkages could influence biological activities. For example, α2,3 linkage may promote selectin binding, and it is related to several cancers and higher patient death rates . Cancer cells are known to have high levels of α2,6-linked sialic acid with galactose the apoptosis inducing galectin proteins interactions with glycan, which improves cell survival . The sialic acid linkage also impacts the anti-inflammatory properties of IgG.