Open AccessPhage display of proteins.
Author(s) -
Katarzyna Kościelska,
Liliana Kiczak,
Monika Kasztura,
Olga Wesołowska,
Jacek Otlewski
Publication year - 1998
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1998_4210
Subject(s) - phage display , computational biology , sequence space , protein engineering , protein design , phagemid , protein folding , directed molecular evolution , function (biology) , biology , directed evolution , computer science , protein structure , genetics , gene , bacteriophage , biochemistry , escherichia coli , antibody , enzyme , mathematics , mutant , pure mathematics , banach space
In recent years the phage display approach has become an increasingly popular method in protein research. This method enables the presentation of large peptide and protein libraries on the surface of phage particles from which molecules of desired functional property(ies) can be rapidly selected. The great advantage of this method is a direct linkage between an observed phenotype and encapsulated genotype, which allows fast determination of selected sequences. The phage display approach is a powerful tool in generating highly potent biomolecules, including: search for specific antibodies, determining enzyme specificity, exploring protein-protein and protein-DNA interactions, minimizing proteins, introducing new functions into different protein scaffolds, and searching sequence space of protein folding. In this article many examples are given to illustrate that this technique can be used in different fields of protein science. The phage display has a potential of the natural evolution and its possibilities are far beyond rational prediction. Assuming that we can design the selection agents and conditions we should be able to engineer any desired protein function or feature.