Development of a small peptide tag for covalent labeling of proteins.
A 21-mer peptide that can be used to covalently introduce synthetic molecules into proteins has been developed. Phage-displayed peptide libraries were subjected to reaction-based selection with 1,3-diketones. The peptide was further evolved by addition of a randomized region and reselection for improved binding. The resulting 21-mer peptide had a reactive amino group that formed an enaminone with 1,3-diketone and was used as a tag for labeling of maltose binding protein. Using this peptide tag and 1,3-diketone derivatives, a variety of molecules such as reporter probes and functionalities may be covalently introduced into proteins of interest.
Tanaka
Fujie
F
The Department of Molecular Biology, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA. ftanaka@scripps.edu
Fuller
Roberta
R
Asawapornmongkol
Lily
L
Warsinke
Axel
A
Gobuty
Sarah
S
Barbas
Carlos F
CF
D002352:Carrier Proteins / Q000737:chemistry*; D007659:Ketones / Q000737:chemistry; D058619:Maltose-Binding Proteins; D019151:Peptide Library; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D011993:Recombinant Fusion Proteins / Q000737:chemistry*
D002352:Carrier Proteins; D007659:Ketones; D058619:Maltose-Binding Proteins; D019151:Peptide Library; D010455:Peptides; D011993:Recombinant Fusion Proteins