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• W3165996927 abstract "Characterization of the protein-peptide interactions are a critical for understanding the functions and signal pathways of proteins. Herein, a new finding of universal terminal protection that protein bind specifically with peptide and provide a protective coating to prevent peptide hydrolysis in the presence of peptidase. On the basis of this mechanism, we first reported a novel label-free fluorescence biosensor strategy that utilizes the protection of specific terminal protein on peptide-templated gold nanocluster (AuNCs) beacon for the detection of proteins. The fluorescence quenching of peptide-templated AuNCs can be effectively inhibited with increasing concentration of the specific protein, exhibiting a satisfactory sensitivity and selectivity toward protein with the detection limit of MDM2 and gp120 are 0.0019 U/mL and 0.0012 U/mL, respectively. The developed label-free fluorescence biosensor strategy provides new ideas to detect and screen protein for analyzing protein-peptide interaction in biomedical applications. • A novel label-free fluorescence biosensor was developed for the detection and screening of protein. • Using MDM2 and gd120 as an example, peptide-templated AuNCs realized its specific determination. • Peptide-templated AuNCs can be applied in the biomedical for the screening of protein." @default.
• W3165996927 created "2021-06-22" @default.
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• W3165996927 date "2021-10-01" @default.
• W3165996927 modified "2023-09-26" @default.
• W3165996927 title "Terminal protection of peptides by interactions with proteins: A “signal-on” peptide-templated gold nanocluster beacon for label-free protein detection" @default.
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• W3165996927 doi "https://doi.org/10.1016/j.talanta.2021.122566" @default.
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