Designing Proteins That Work Using Recombinant Technologies

Author(s): T. J. Graddis, R. L. Remmele Jr., J. T. McGrew.

Journal Name: Current Pharmaceutical Biotechnology

Volume 3 , Issue 4 , 2002

Become EABM
Become Reviewer


Therapeutic proteins have been engineered for a variety of purposes including reduced antigenicity, longer halflife, 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.

Keywords: Proteins

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2002
Page: [285 - 297]
Pages: 13
DOI: 10.2174/1389201023378148
Price: $65

Article Metrics

PDF: 6