Optical biosensors based on one-dimensional photonic crystals sustaining Bloch surface waves are proposed to study antibody interactions and perform affinity studies. The presented approach utilizes two types of different antibodies anchored at the sensitive area of a photonic crystal-based biosensor. Such a strategy allows for creating two or more on-chip regions with different biochemical features as well as studying the binding kinetics of biomolecules in real time. In particular, the proposed detection system shows an estimated limit of detection for the target antibody (anti-human IgG) smaller than 0.19 nM (28 ng/mL), corresponding to a minimum surface mass coverage of 10.3 ng/cm2. Moreover, from the binding curves we successfully derived the equilibrium association and dissociation constants (KA = 7.5 × 107 M−1; KD = 13.26 nM) of the human IgG–anti-human IgG interaction.
Label-free monitoring of human IgG/anti-IgG recognition using Bloch surface waves on 1D photonic crystals / Sinibaldi, Alberto; Occhicone, Agostino; Munzert, Peter; Danz, Norbert; Sonntag, Frank; Michelotti, Francesco. - In: BIOSENSORS. - ISSN 2079-6374. - 8:(2018). [10.3390/bios8030071]
Label-free monitoring of human IgG/anti-IgG recognition using Bloch surface waves on 1D photonic crystals
Sinibaldi, Alberto
Primo
;Occhicone, Agostino;Michelotti, FrancescoUltimo
2018
Abstract
Optical biosensors based on one-dimensional photonic crystals sustaining Bloch surface waves are proposed to study antibody interactions and perform affinity studies. The presented approach utilizes two types of different antibodies anchored at the sensitive area of a photonic crystal-based biosensor. Such a strategy allows for creating two or more on-chip regions with different biochemical features as well as studying the binding kinetics of biomolecules in real time. In particular, the proposed detection system shows an estimated limit of detection for the target antibody (anti-human IgG) smaller than 0.19 nM (28 ng/mL), corresponding to a minimum surface mass coverage of 10.3 ng/cm2. Moreover, from the binding curves we successfully derived the equilibrium association and dissociation constants (KA = 7.5 × 107 M−1; KD = 13.26 nM) of the human IgG–anti-human IgG interaction.File | Dimensione | Formato | |
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