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.

蛋白质-肽相互作用的表征对于理解蛋白质的功能和信号通路至关重要。在此，新发现的通用末端保护是蛋白质与肽特异性结合并提供保护涂层以防止肽酶存在下肽水解。基于这种机制，我们首先报道了一种新型的无标记荧光生物传感器策略，该策略利用肽模板金纳米簇（AuNCs）信标上特定末端蛋白质的保护来检测蛋白质。随着特定蛋白质浓度的增加，肽模板化AuNCs的荧光猝灭可以被有效抑制，对蛋白质表现出令人满意的灵敏度和选择性，MDM2和gp120的检测限分别为0.0019 U/mL和0.0012 U/mL，分别。开发的无标记荧光生物传感器策略为检测和筛选蛋白质以分析生物医学应用中的蛋白质 - 肽相互作用提供了新的思路。