New methods for efficient protein production in drug discovery

作者：Leder Lukas^*; Freuler Felix; Forstner Michael; Mayr Lorenz M

来源：Current Opinion in Drug Discovery & Development, 2007, 10(2): 193-202.

• affinity purification
• baculovirus
• Escherichia coli
• mammalian cells
• recombinant protein expression
• site-specific modification

The requirement for high levels of stable and functional proteins remains a bottleneck in many processes of modern drug discovery, including the high-throughput screening for novel active compounds or the determination of protein structures. Recently, numerous developments have been made to improve the production of soluble and active proteins in heterologous expression systems. These include versatile expression vectors, new methods for quick cloning, the introduction of novel and/or improved prokaryotic and eukaryotic expression systems, and more efficient and faster chromatographic procedures that result in highly pure proteins. In addition, several techniques allow the attachment of small molecular labels to proteins in a site-specific manner, which can be highly useful for various important experimental techniques in current drug discovery.

• 出版日期2007-3