Mechanisms Leading to an Oriented Immobilization of Recombinant Proteins Derived from the P24 Capsid of HIV-1 onto Copolymers
| Autor: | Guy Oriol, Scrémin G, T. Delair, Bernard Mandrand, François Mallet, Laurent Veron, Merlier F, Cheynet, Laure Allard |
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| Rok vydání: | 2001 |
| Předmět: |
Polymers
Molecular Sequence Data Lysine HIV Core Protein p24 Biomedical Engineering Pharmaceutical Science Bioengineering law.invention law Humans Reactivity (chemistry) Amino Acid Sequence Maleic Anhydrides Pharmacology chemistry.chemical_classification Organic Chemistry Cationic polymerization Polymer Combinatorial chemistry Recombinant Proteins Amino acid Cross-Linking Reagents Capsid chemistry Biochemistry Covalent bond Recombinant DNA Oligopeptides Sequence Alignment Biotechnology |
| Zdroj: | Bioconjugate Chemistry. 12:972-979 |
| ISSN: | 1520-4812 1043-1802 |
| DOI: | 10.1021/bc010042s |
| Popis: | To investigate the mechanism leading to an oriented immobilization of recombinant proteins onto synthetic copolymers, five genetically modified HIV-1 p24 capsid proteins (RH24, RH24A4K2, RH24R6, RH24R4K2, and RH24K6) were tested for their efficiency to covalently bind to maleic anhydride-alt-methyl vinyl ether (MAMVE) and N-vinyl pyrrolidone-alt-maleic anhydride (NVPMA) copolymers. These proteins contain, at their C-termini, tags differing in cationic and/or reactive amino acids density. We demonstrated that an increase of the charge and amine density in the tag enhances the coupling yield, the most efficient tag being a six lysine one. The reactivity of the proteins depends directly on the reactivity of the tag, and this led us to conclude that the tag was the site where the covalent grafting with the polymer occurred. Thus, design of such tags provides a new efficient and versatile method allowing oriented immobilization of recombinant proteins onto copolymers. |
| Databáze: | OpenAIRE |
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