Molecular imprinting of AMP by an ionic-noncovalent dual approach.
In order to mimic recognition properties of adenylate kinase, molecularly imprinted polymers (MIPs) were prepared for adenosine 5'-monophosphate (AMP), a substrate of the enzyme. Different functional monomers interacting with the phosphate moiety were tested, and the MIP giving the best specific binding of AMP was composed with one equivalent of 2-(dimethylamino)ethyl methacrylate and ten equivalents of acrylamide compared to AMP. Packed into solid phase cartridge, this polymer showed similar characteristics than the enzyme, since it was specific for AMP toward other nucleotides.
Breton
Florent
F
Institut de Chimie Organique et Analytique, UMR 6005, Université d'Orléans, Orléans, France.
Delépée
Raphaël
R
Agrofoglio
Luigi A
LA
D000249:Adenosine Monophosphate / Q000737:chemistry* / Q000378:metabolism; D000263:Adenylate Kinase / Q000737:chemistry / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid / Q000295:instrumentation / Q000379:methods; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007477:Ions; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D054802:Molecular Imprinting; D015394:Molecular Structure; D011108:Polymers / Q000737:chemistry*; D011485:Protein Binding
D007477:Ions; D007527:Isoenzymes; D011108:Polymers; D000249:Adenosine Monophosphate; D000263:Adenylate Kinase