Electrostatically driven immobilization of peptides onto (Maleic anhydride-alt-methyl vinyl ether) copolymers in aqueous media.
The covalent immobilization of a model peptide onto the MAMVE copolymer, via the formation of amide bonds, occurred in moderate yields in aqueous conditions. The improvement of the grafting reaction was achieved by adding at the amino terminus of the model peptide a sequence (tag) of three positively charged amino acids, lysine or arginine, and by taking profit of electrostatic attractive interactions between the negatively charged copolymer and the tagged peptides. The arginine tag was more efficient than the lysine tag for enhancing the immobilization reaction, proving that the effect was due to an electrostic driving force. On the basis of these results, a tentative mechanism is discussed, and Scatchard plots pointed out two regimes of binding. With the first, at low polymer load (up to 50% of saturation for a lysine tag and 60-70% for an arginine tag), the binding occurred with a positive cooperative effect, the already bound peptide participating to the binding of others. A second one for higher coverages, for which the binding occurred with a negative cooperativity, and saturation was reached in the presence of a large excess of peptide.
Ladavière
C
C
Unité Mixte UMR-103, CNRS-bioMérieux, ENS-Lyon, 46, allée d'Italie, 69364 Lyon, France.
Lorenzo
C
C
Elaïssari
A
A
Mandrand
B
B
Delair
T
T
D000595:Amino Acid Sequence; D007700:Kinetics; D008298:Maleates / Q000737:chemistry*; D008956:Models, Chemical; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry*; D011095:Polyethylenes / Q000737:chemistry*; D055672:Static Electricity; D014867:Water
D008298:Maleates; D009842:Oligopeptides; D011095:Polyethylenes; D014867:Water; C043105:poly(methyl vinyl ether-co-maleic anhydride)