Fig. 1: Construction of complexes, and proposed mechanism(s) underlying intracellular delivery of genome-editing ribonucleoproteins (RNPs) mediated by Coomassie Brilliant Blue (CBB) liposomes. | Nature Communications

Fig. 1: Construction of complexes, and proposed mechanism(s) underlying intracellular delivery of genome-editing ribonucleoproteins (RNPs) mediated by Coomassie Brilliant Blue (CBB) liposomes.

From: A combinatorial synthetic strategy for developing genome-editing protein-delivery agents targeting mouse retina

Fig. 1: Construction of complexes, and proposed mechanism(s) underlying intracellular delivery of genome-editing ribonucleoproteins (RNPs) mediated by Coomassie Brilliant Blue (CBB) liposomes.

The fundamental design principles for a CBB-containing delivery agent include: (1) the CBB protein-binding domain; (2) an ionizable-linker domain; and (3) a lipid or lipidoid domain. The CBB compounds are integrated into liposomes comprising ionizable lipid (orange), phospholipid (grey), cholesterol (red) and PEG lipid (light blue), and bind RNP on the liposome surface in an aqueous, neutral environment. The RNP-liposome complex is absorbed by the cells via the endocytosis pathway. Subsequent protonation of the ionizable CBB delivery agents and ionizable lipids releases the tagged proteins from the particles, enabling their intracellular transport to the nucleus to edit the targeted DNA sequence.

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