Designing proteins that work using recombinant technologies
| Autor: | J. T. McGrew, R. L. Remmele, T. J. Graddis |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Glycosylation
Rational design Pharmaceutical Science Proteins Protein engineering Computational biology Biology Directed evolution Bioinformatics Protein Engineering Fusion protein Recombinant Proteins DNA shuffling law.invention chemistry.chemical_compound chemistry law Recombinant DNA PEGylation Animals Humans Technology Pharmaceutical Biotechnology |
| Zdroj: | Current pharmaceutical biotechnology. 3(4) |
| ISSN: | 1389-2010 |
| Popis: | Therapeutic proteins have been engineered for a variety of purposes including reduced antigenicity, longer half-life, simplified process development, and increased affinity. Fusion proteins bring together functions from two different molecules creating therapeutics with completely novel activities. Protein engineering technologies have relied on rational design, directed evolution, DNA shuffling, RNA-peptide fusion, phage and ribosomal display methods to select out candidate protein forms with the desired therapeutic properties. Engineered site-specific pegylation and glycosylation strategies have improved circulation half-life, reduced immunogenicity and increased protein therapeutic stability. In this review we describe how protein engineering techniques have been used to select out, improve stability and clinical efficacy of protein therapeutics. |
| Databáze: | OpenAIRE |
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