title: Sequence-Specific 2-Cyanobenzothiazole Ligation.
abstract: The use of small, natural chemical reporters in conjunction with catalyst-free bioorthogonal reactions will greatly streamline protein labeling in a cellular environment with minimum perturbation to their function. Here we report the discovery of a 2-cyanobenzothiazole (CBT)-reactive peptide tag, CX10R7, from a cysteine-encoded peptide phage library using the phage-assisted interrogation of reactivity method. Fusion of CX10R7 with a protein of interest allows site-specific labeling of the protein with CBT both in vitro and on the surface of E. coli cells. Mutagenesis studies indicated that the reactivity and specificity of CX10R7 are attributed to the sequence environment, in which the residues surrounding cysteine help to stabilize the ligation product.
authors.affiliation: Department of Chemistry, State University of New York at Buffalo , Buffalo, New York 14260, United States.
authors.forename: Carlo P
authors.initials: CP
authors.lastname: Ramil
authors.affiliation: Department of Chemistry, State University of New York at Buffalo , Buffalo, New York 14260, United States.
authors.forename: Peng
authors.initials: P
authors.lastname: An
authors.affiliation: Department of Chemistry, State University of New York at Buffalo , Buffalo, New York 14260, United States.
authors.forename: Zhipeng
authors.initials: Z
authors.lastname: Yu
authors.affiliation: Department of Chemistry, State University of New York at Buffalo , Buffalo, New York 14260, United States.
authors.forename: Qing
authors.initials: Q
authors.lastname: Lin
mesh_terms: D000595:Amino Acid Sequence; D052160:Benzothiazoles / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D009570:Nitriles / Q000737:chemistry* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry*
chemical_list: C578355:2-cyanobenzothiazole; D052160:Benzothiazoles; D009570:Nitriles; D010455:Peptides