Novel peptide surface for reversible immobilization of concanavalin A.
Concanavalin A (Con A) was spontaneously adsorbed on polymyxin B surface. This peptide-lectin interaction was strong, K(D)=1.9 x 10(-10), based predominantly on creation of hydrophobic bonds, and was completely reversible. Concanavalin A on polymyxin B (PmB) retained higher binding capacity for yeast mannan, compared with covalently immobilized lectin. Kinetics of mannan-concanavalin A interaction were significantly different in dependence on type of concanavalin A immobilization.
Masárová
Jana
J
Pure and Applied Biochemistry, LTH, Lund University, S-22100, Sweden. jana.masarova@tbiokem.lth.se
Dey
Estera Szwajcer
ES
Carlsson
Jenny
J
Danielsson
Bengt
B
D000327:Adsorption; D001703:Biophysics / Q000379:methods; D003208:Concanavalin A / Q000032:analysis / Q000737:chemistry*; D007700:Kinetics; D008351:Mannans / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011112:Polymyxin B / Q000737:chemistry*; D011485:Protein Binding; D020349:Surface Plasmon Resonance; D013997:Time Factors; D015003:Yeasts / Q000378:metabolism
D008351:Mannans; D010455:Peptides; D003208:Concanavalin A; D011112:Polymyxin B