title: Production of prone-to-aggregate proteins.
abstract: Expression of recombinant proteins in Escherichia coli (E. coli) remains the most popular and cost-effective method for producing proteins in basic research and for pharmaceutical applications. Despite accumulating experience and methodologies developed over the years, production of recombinant proteins prone to aggregate in E. coli-based systems poses a major challenge in most research applications. The challenge of manufacturing these proteins for pharmaceutical applications is even greater. This review will discuss effective methods to reduce and even prevent the formation of aggregates in the course of recombinant protein production. We will focus on important steps along the production path, which include cloning, expression, purification, concentration, and storage.
authors.affiliation: Protein Expression and Purification Facilities, Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Jerusalem, Israel. Electronic address: mario.l@mail.huji.ac.il.
authors.forename: Mario
authors.initials: M
authors.lastname: Lebendiker
authors.affiliation: Protein Expression and Purification Facilities, Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Jerusalem, Israel.
authors.forename: Tsafi
authors.initials: T
authors.lastname: Danieli
mesh_terms: D005818:Genetic Engineering / Q000379:methods*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D011994:Recombinant Proteins
keywords: Aggregation analysis; Aggregation suppressor; Buffer condition; Chaotrope; Chaperone; Fusion protein; Induction condition; Intrinsically disordered protein; Intrinsically disordered region; Kosmotrope; Protein aggregation; Protein concentration; Protein storage; Stabilizer