Charges drive selection of specific antibodies by phage display.
Phage display technology has emerged as a leading approach to select proteins with improved properties for many different types of applications. The selection typically selects not only for improved binding properties but also for other factors such as efficiency of protein production and folding in Escherichia coli, the host in which the proteins and the phage are produced. Furthermore, the selection methodology is likely to influence the character of retrieved variants. We have now defined the extent whereby the charge of the displayed proteins influence the selection process, resulting in an increased average positive charge among selected proteins in comparison to the proteins that are harbored in the library before selection. Implications of and possible routes to minimize this effect are discussed.
Persson
Helena
H
Department of Immunotechnology, Lund University, BMC D13, SE-221 84 Lund, Sweden.
Persson
Jonas
J
Danielsson
Lena
L
Ohlin
Mats
M
D000595:Amino Acid Sequence; D000915:Antibody Affinity; D000918:Antibody Specificity; D019921:Biotinylation; D022801:Complementarity Determining Regions / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009994:Osmolar Concentration; D019151:Peptide Library; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D012965:Sodium Chloride / Q000737:chemistry; D013499:Surface Properties
D022801:Complementarity Determining Regions; D019151:Peptide Library; D011994:Recombinant Proteins; D012965:Sodium Chloride