title: Genetic incorporation of 1,2-aminothiol functionality for site-specific protein modification via thiazolidine formation.
abstract: Here we report a new site-specific conjugation strategy to modify proteins via thiazolidine ligation. Proteins harbouring a 1,2-aminothiol moiety introduced by amber codon suppression technology could be modified chemoselectively with aldehyde-functionalized reagents, such as a biotin-labeled peptide or ubiquitin, under mild conditions to yield homogeneous biotinylated or ubiquitinated products.
authors.affiliation: Division of Structural Biology and Biochemistry, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore. cfliu@ntu.edu.sg.
authors.forename: Xiaobao
authors.initials: X
authors.lastname: Bi
authors.forename: Kalyan Kumar
authors.initials: KK
authors.lastname: Pasunooti
authors.forename: Ahmad Hussen
authors.initials: AH
authors.lastname: Tareq
authors.forename: John
authors.initials: J
authors.lastname: Takyi-Williams
authors.forename: Chuan-Fa
authors.initials: CF
authors.lastname: Liu
mesh_terms: D000447:Aldehydes / Q000737:chemistry; D019921:Biotinylation; D003062:Codon / Q000235:genetics*; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D053778:Thiazolidines / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D000447:Aldehydes; D003062:Codon; D011506:Proteins; D013438:Sulfhydryl Compounds; D053778:Thiazolidines