title: Novel peptide surface for reversible immobilization of concanavalin A.
abstract: 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.
authors.affiliation: Pure and Applied Biochemistry, LTH, Lund University, S-22100, Sweden. jana.masarova@tbiokem.lth.se
authors.forename: Jana
authors.initials: J
authors.lastname: Masárová
authors.forename: Estera Szwajcer
authors.initials: ES
authors.lastname: Dey
authors.forename: Jenny
authors.initials: J
authors.lastname: Carlsson
authors.forename: Bengt
authors.initials: B
authors.lastname: Danielsson
mesh_terms: 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
chemical_list: D008351:Mannans; D010455:Peptides; D003208:Concanavalin A; D011112:Polymyxin B