This unit describes the process and analysis of affinity selecting bacteriophage M13 from libraries displaying combinatorial peptides fused to either a minor or major capsid protein. Direct affinity selection uses target protein bound to a microtiter plate followed by purification of selected phage by ELISA. Alternatively, there is a bead-based affinity selection method. These methods allow one to readily isolate peptide ligands that bind to a protein target of interest and use the consensus sequence to search proteomic databases for putative interacting proteins.
Kay, B., Castagnoli, L. (2003). Mapping protein-protein interactions with phage-displayed combinatorial peptide libraries. CURRENT PROTOCOLS IN CELL BIOLOGY, Chapter 17, Unit 17.4-Unit 17.4 [10.1002/0471143030.cb1704s17].
Mapping protein-protein interactions with phage-displayed combinatorial peptide libraries
CASTAGNOLI, LUISA
2003-02-02
Abstract
This unit describes the process and analysis of affinity selecting bacteriophage M13 from libraries displaying combinatorial peptides fused to either a minor or major capsid protein. Direct affinity selection uses target protein bound to a microtiter plate followed by purification of selected phage by ELISA. Alternatively, there is a bead-based affinity selection method. These methods allow one to readily isolate peptide ligands that bind to a protein target of interest and use the consensus sequence to search proteomic databases for putative interacting proteins.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.