These kinetic results agree well with the different binding modes of the three lectins. The simultaneous binding mode of DC-SIGN and DC-SIGN-C provides a rapid interaction where, once initial contact between a CRD and QD-DiMan is formed, it becomes kinetically more favourable for the other CRDs in the same lectin to bind due to their close proximity with the ligand. For DC-SIGNR, due to the similar magnitudes of the 𝑘 𝑜𝑛 terms for the three proteins, it is likely that the initial rapid increase in binding is a result of the simultaneous binding of two CRDs with one QD-DiMan to form a QD-DC-SIGNR intermediate unit. The secondary increase in binding, occuring over a much longer timescale, can be attributed to inter-cross-linking interactions. As inter-cross-linking requires multiple QD-lectin units (QD with divalently bound lectin) to interact with each other to form large assemblies, it would be a much slower process.