Related Experiment Video
Updated: Jun 7, 2026
Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
Published on: August 20, 2018
Perfluorophenyl azide immobilization chemistry for single molecule force spectroscopy of the concanavalin A/mannose
Carolin Madwar1, William Chu Kwan, Lingquan Deng
1Department of Chemistry & Biochemistry, Concordia University, 7141 Sherbrooke Street West, Montréal, Québec, Canada H4B 1R6.
Abstract:
The versatility of perfluorophenyl azide (PFPA) derivatives makes them useful for attaching a wide variety of biomolecules and polymers to surfaces. Herein, a single molecule force spectroscopy (SMFS) study of the concanavalin A/mannose interaction was carried out using PFPA immobilization chemistry. SMFS of the concanavalin A/mannose interaction yielded an average unbinding force of 70-80 pN for loading rates between 8000 and 40,000 pN/s for mannose surfaces on aminated glass, and an unbinding force of 57 ± 20 pN at 6960 pN/s for mannose surfaces on gold-coated glass. Dynamic force spectroscopy was used to determine the dissociation rate constant, k(off), for this interaction to be 0.16 s(-1).
