3.2.1. Lectin biosensor:
Lectin-based biosensors determines the measurable signal by estimating
the conversion of lectin-carbohydrate interactions. Lectins have a high
affinity to multivalent oligosaccharides. Lectins’ extremely specific
binding to terminal carbohydrate moieties on cell surfaces and protein
aggregates is used in physiological and pathological studies, such as
virus and bacterium detection and glycol profiling of serum
glycoproteins. Electrochemical lectin-based biosensors can be used to
diagnose illness and pathogens by detecting biomarkers (Coelho et al.,
2017), as well as biorecognition of glycan in viral proteins (Cesewski
& Johnson, 2020).
SARS-COV-2 envelope glycoprotein might be exploited for early detection
using lectin-based biosensors. Another use of lectin-based
electrochemical biosensors includes the use of cyclic voltammetry and
impedance to detect norovirus (nonenveloped virus) in feces samples
without showing cross-reactivity with hepatitis A or E (Hong et al.,
2015). The impedimetric lectin-based biosensor can also be applied for
differentiating chikungunya virus, Zika virus, yellow fever and DENV-2
in serum-based samples (Simao et al., 2020).
Liao et al. (2016) described a lectin-based biosensor made from the
marine mollusk Crenomytilus grayanus (CG) that may be used to
diagnose and treat cancer. The CGL crystal can attach to three ligands:
galactose, galactosamine, and globotriose (Gb3), and it may be utilized
to recognize Gb3 on the surface of breast cancer cells, causing them to
die. Peiris et al. (2012) developed a lectin-based biosensor using
N-acetylgalactosamine lectin from the Roman snail Helix pomatia
agglutinin (HPA) (Helix pomatia). This HPA based biosensor can have an
affinity for metastatic SW620 cells and non-metastatic SW480 in
different molar ranges.
This approach is the latest approach for the selective determination and
quantification of cancer-specific glycans and lectin.