Products | SPR Sensor chips | Data sheets

ZC–modified sensor chips (Zwitterionic)

XanTec’s ZC sensor chips are coated with a zwitterionic polymer comprising an approximately equimolar ratio of carboxylic acid and tertiary amine groups. The resulting near-neutral net charge renders the surface highly bioinert toward charge-driven nonspecific binding.

ZC sensor chips support efficient EDC/NHS-based covalent coupling through a transient charge-shift mechanism. During activation, negatively charged carboxyl groups are converted into charge-neutral NHS esters, shifting the net surface charge toward positive. In this activated state, reversed-charge electrostatic preconcentration occurs, favoring enrichment of negatively charged ligands. After coupling, hydrolysis or quenching (e.g., with glycine) restores the charge-neutral zwitterionic surface.

These properties make ZC sensor chips particularly suitable for immobilizing acidic ligands, ligands unstable under acidic preconcentration conditions, and for analyzing strongly cationic analytes that would otherwise bind nonspecifically to classic polycarboxylate coatings such as CMD or HC.

Key features:

Schematic illustration of the reversed-charge preconcentration approach (panels numbered 1–4 from left to right).1

1. Native ZC sensor chip: Red and blue dots represent carboxyl and tertiary amine groups evenly distributed along the green polymer chains.
2. EDC/NHS activation: A fraction of the negatively charged carboxyl groups are converted into charge-neutral NHS esters (yellow), transiently shifting the net surface charge toward positive.
3. Reversed-charge preconcentration and coupling: Ligands with a negative net charge (cyan) accumulate at the surface via reversed-charge electrostatic preconcentration and are subsequently covalently immobilized through formation of amide bonds.
4. Deactivation: Hydrolysis or quenching (e.g., with 1 M glycine at pH 8.5) converts remaining NHS esters back into carboxylic acids, restoring the charge-neutral surface.
Product code ZC30M ZC80M ZC150D ZCC150D
Base coating 3D, 30 nm bioinert charge-neutral zwitterionic polymer (medium density) 3D, 80 nm bioinert charge-neutral zwitterionic polymer (medium density) 3D, 150 nm bioinert charge-neutral zwitterionic polymer (high density) 3D, 150 nm bioinert charge-positive zwitterionic polymer (high density)
Covalent immobilization capacity [µRIU]2 ≈ 2,600 (3,000) ≈ 6,000 (7,000) ≈ 22,000 (30,000) ≈ 0 (30,000)
Recommended ligands3
  • proteins with low to slightly basic pI (< 7.5)
  • (acidic) peptides
  • nucleic acids
  • (acidic) carbohydrates with NHS-reactive amino group
Recommended analytes
  • proteins
  • peptides
  • nucleic acids
  • viruses and cells
  • carbohydrates
  • proteins
  • peptides
  • nucleic acids
  • small molecules
  • carbohydrates
  • peptides
  • nucleic acids
  • small molecules
  • fragments
  • carbohydrates
  • peptides
  • nucleic acids
  • small molecules
  • fragments
  • carbohydrates
Intended purpose
  • immobilization of acidic biomolecules
  • immobilization at neutral pH
  • reduced nonspecific binding
  • kinetics of medium and large analytes
  • immobilization of acidic biomolecules
  • neutral pH immobilization
  • reduced nonspecific binding
  • kinetics of medium analytes
  • immobilization of acidic biomolecules
  • neutral pH immobilization
  • reduced nonspecific binding
  • reusable high-capacity surface
  • electrostatic preconcentration scouting
  • not intended for permanent covalent immobilization

1 All illustrations are schematic representations and are not drawn to scale; dimensions, densities, and spatial relationships do not reflect actual physical or chemical proportions.

2 Typical covalent immobilization capacity and electrostatic preconcentration capacity (in brackets) determined by injecting 100 µg/mL Protein A in 10 mM MES buffer (pH 6.5) following surface activation with 0.5 M EDC in NHS/MES activation buffer.

3 All ligands require at least one NHS-reactive amino group.