| Autor: |
Reddy, Neelesh C., Molla, Rajib, Joshi, Pralhad Namdev, T. K., Sajeev, Basu, Ipsita, Kawadkar, Jyotsna, Kalra, Neetu, Mishra, Ram Kumar, Chakrabarty, Suman, Shukla, Sanjeev, Rai, Vishal |
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| Zdroj: |
Nature Communications; 10/13/2022, Vol. 13 Issue 1, p1-15, 15p |
| Abstrakt: |
The maintenance of machinery requires its operational understanding and a toolbox for repair. The methods for the precision engineering of native proteins meet a similar requirement in biosystems. Its success hinges on the principles regulating chemical reactions with a protein. Here, we report a technology that delivers high-level control over reactivity, chemoselectivity, site-selectivity, modularity, dual-probe installation, and protein-selectivity. It utilizes cysteine-based chemoselective Linchpin-Directed site-selective Modification of lysine residue in a protein (LDMC-K). The efficiency of the end-user-friendly protocol is evident in quantitative conversions within an hour. A chemically orthogonal C-S bond-formation and bond-dissociation are essential among multiple regulatory attributes. The method offers protein selectivity by targeting a single lysine residue of a single protein in a complex biomolecular mixture. The protocol renders analytically pure single-site probe-engineered protein bioconjugate. Also, it provides access to homogeneous antibody conjugates (AFC and ADC). The LDMC-K-ADC exhibits highly selective anti-proliferative activity towards breast cancer cells. Controlling the selectivity of the chemical modification of a genetic-manipulation-free protein is currently problematic. Here the authors report a method using cysteine-based chemoselective Linchpin Directed site-selective Modification of the lysine residue in a protein. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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