Construction of an Entropy-Driven Dumbbell-Type DNAzyme Assembly Circuit for Lighting Up Uracil-DNA Glycosylase in Living Cells

Key Words:BETA-PEPTIDES; IN-VITRO; PROTEOLYTIC STABILITY; GAMMA-PEPTIDES; AMINO-ACIDS; ANTIBACTERIAL; GLYCOSYLATION; SEQUENCE

Abstract:The zwitterionic peptides, especially those composed of glutamic (E) and lysine (K) groups have drawn enormous attention as antifouling biomaterials owing to their strong hydration capability and biocompatibility. However, the susceptibility of alpha-amino acid K to the proteolytic enzymes in human serum limited the broad application of such peptides in biological media. Herein, a new multifunctional peptide with favorable stability in human serum was designed, and it was composed of three sections with immobilizing, recognizing and antifouling capabilities, respectively. The antifouling section was composed of alternating E and K amino acids, but the enzymolysis-susceptive amino acid alpha-K was replaced by the unnatural beta-K. Compared with the conventional peptide composed of all alpha-amino acids, the alpha/beta-peptide exhibited significantly enhanced stability and longer antifouling performance in human serum and blood. The electrochemical biosensor based on the alpha/beta-peptide showed a favorable sensitivity to its target IgG, with a quite wide linear range from 100 pg mL(-1) to 10 mu g mL(-1) and a low detection limit (33.7 pg mL(-1), S/N = 3), and it was promising for the detection of IgG in complex human serum. The tactic of designing antifouling alpha/beta-peptides offered an efficient way to develop low-fouling biosensors with robust operation in complex body fluids.

Volume:1263

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Translation or Not:no