| Literature DB >> 31657212 |
Qing Zhang1, Yue Zhang1, Heng Liu1, Hoi Yee Chow1, Ruijun Tian2, Yi Man Eva Fung1, Xuechen Li1.
Abstract
Lysine residues have been considered as a routine conjugating site for protein chemical labeling and modification. The commercially available lysine-labeling agents have several limitations in labeling efficiency, stability, and cost. To pursue alternative protein lysine-labeling strategies, herein, we report the development of an ortho-phthalaldehyde (OPA)-based bifunctional linker suitable for protein chemical labeling and profiling. Among three designed OPA-based bifunctional linkers, OPA-NH-alkyne 5 was proved to be optimal for protein labeling with minimal protein turbidity. We further demonstrated OPA-NH-alkyne 5 was applicable for immediate capture of protein or proteome chemical labeling.Entities:
Year: 2019 PMID: 31657212 DOI: 10.1021/acs.biochem.9b00787
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162