Surface modification of proteins by covalent binding of acrylic polymers |
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| Authors: | Francesco M. Veronese Roberta Largajolli Carlo Visco Paolo Ferruti Adelaide Miucci |
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| Affiliation: | (1) Department of Pharmaceutical Sciences (Centro di Studi per la Chimica del Farmaco e dei Prodotti Biologicamente Attivi del CNR), University of Padua, Padua, Italy;(2) Faculty of Engineering, University of Brescia, Brescia, Italy;(3) Department of Industrial Chemistry, Chemical Engineering-Polytechnic of Milan, Milan, Italy |
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| Abstract: | Surface modification of enzymes for a potential use in therapy was obtained with a new type of tailor-made copolymers ofNacryloylmorpholine andN-acryloxysuccinimide. The first monomer was designed to confer solubility on the polymer, whereas the second was used to give it reactivity toward protein amino groups. The reactivity of polymers of different composition towards amino acid derivatives and model proteins, such as catalase and ribonuclease-A, is described. Water soluble and catalytically active enzyme derivatives were obained using copolymers prepared with a mixture of N-acryloxysuccinimide andn-acryloylmorpholine in a 1:99 molar ratio. At increasing molar ratio (3:97, 10:90) extensive crosslinking between polymer and enzymes takes place, yielding insoluble adducts. |
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| Keywords: | Protein surface modification, by acryloylmorpholine-acryloxysuccinimide copolymers ribonuclease-A, and catalase modification by soluble polyacrylic polymers modification, of therapeutically useful enzymes by polyacrylic polymers surface modification, of proteins by acrylic polymers acrylic polymers |
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