Perfluorophenyl azide immobilization chemistry for single molecule force spectroscopy of the concanavalin A/mannose interaction.
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).
Department of Chemistry & Biochemistry, Concordia University, 7141 Sherbrooke Street West, Montréal, Québec, Canada H4B 1R6.
Carolin
C
Madwar
William Chu
WC
Kwan
Lingquan
L
Deng
Olof
O
Ramström
Rolf
R
Schmidt
Shan
S
Zou
Louis A
LA
Cuccia
D001386:Azides / Q000737:chemistry*; D003208:Concanavalin A / Q000378:metabolism*; D006845:Hydrocarbons, Fluorinated / Q000737:chemistry*; D008358:Mannose / Q000737:chemistry* / Q000378:metabolism*; D018625:Microscopy, Atomic Force; D055668:Photochemical Processes; D011485:Protein Binding; D013499:Surface Properties
D001386:Azides; D006845:Hydrocarbons, Fluorinated; C556136:perfluorophenyl azide; D003208:Concanavalin A; D008358:Mannose