期刊
BIOCONJUGATE CHEMISTRY
卷 25, 期 6, 页码 1172-1180出版社
AMER CHEMICAL SOC
DOI: 10.1021/bc500195w
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资金
- Ministry of Science and Technology Basic Research Program [2011CB809100]
- National Natural Science Foundation of China [21272016, 21002003, 91013003, J1030413]
- Beijing Nova Program [2010B002]
- Doctoral Fund of Ministry of Education of China [20120001110083]
Characterization of small molecule (SM)-protein interaction is of high importance in biomedical research such as target identification and proteomic profiling. Photo-cross-linking is a powerful and straightforward strategy to covalently capture SM's binding proteins. The DNA-based photoaffinity labeling method is able to capture SM's protein targets with high specificity but suffers low cross-linking efficiency, which limits its utility for low abundance and low affinity proteins. After screening a variety of cross-linkers, by utilizing the multivalency effect, the cross-linking efficiency was improved by nearly 7-fold without compromising probe specificity. The generality and performance of multivalent photoaffinity probes have been validated with a variety of SM-protein pairs in the complexity of cell lysates.
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