Biophysical characterization methods such as surface plasmon resonance (SPR) are powerful tools for characterizing molecular interactions and binding mechanisms, including antibody-antigen, protein-drug and protein-protein interactions.

When used to analyze antibody-antigen interactions, SPR data can help scientists select antibodies with optimal characteristics for their specific applications. The equilibrium dissociation constant (KD), for example, can be used to assess antibody affinity and sensitivity.

Recently, Cayman scientists used the SPR method to characterize the binding kinetics and affinities of several of their anti-ganglioside monoclonal antibodies with their respective antigens using Biacore technologies:

Monoclonal Antibody	Clone	Antigene	KD	Reference
Ganglioside GD1a	MOG35	Ganglioside GD1a (bovine brain) (sodium salt)	2.01 μM	38295
Ganglioside GD1a	TBG3	Ganglioside GD1a (bovine brain) (sodium salt)	1.36 μM	38296
Ganglioside GD1b	MOG1	Ganglioside GD1b (porcine) (sodium salt)	0.052 μM	38293
Ganglioside GM1	DG2	Ganglioside GM1 (porcine brain) (sodium salt)	1.81 μM	38290
Ganglioside GQ1b	CGM3	Ganglioside GQ1b Mixture (sodium salt)	8.18 μM	38287