Data from: Designing fluorescent peptide sensors with dual specificity for the detection of HIV-1 protease

Attached file provides supplementary data for linked article.

HIV-1 protease is a key enzyme in the life cycle of HIV/AIDS, as it is responsible for the formation of the mature virus particle. We demonstrate here that phage-display peptides raised against this enzyme can be used as peptide sensors for the detection of HIV-1 protease in a simple, one-pot assay. The presence of the enzyme is detected through an energy transfer between two peptide sensors when simultaneously complexed with the target protein. The multivalent nature of this assay increases the specificity of the detection by requiring all molecules to be interacting in order for there to be a FRET signal. We also perform molecular dynamics simulations to explore the interaction between the protease and the peptides in order to guide the design of these peptide sensors and to understand the mechanisms which cause these simultaneous binding events. This approach aims to facilitate the development of new assays for enzymes that are not dependent on the cleavage of a substrate and do not require multiple washing steps.

附件文件为关联论文提供补充数据。HIV-1蛋白酶（HIV-1 protease）是HIV/AIDS生命周期中的关键酶，负责成熟病毒颗粒的组装形成。本研究证实，针对该酶筛选得到的噬菌体展示肽可作为肽传感器，通过简便的单管一步检测法实现对HIV-1蛋白酶的检测。当两种肽传感器同时与靶蛋白结合时，可通过二者间的能量转移信号检测该酶的存在。该检测方法的多价特性要求所有分子均发生相互作用方可产生FRET（荧光共振能量转移）信号，从而提升了检测的特异性。本研究同时开展分子动力学模拟，以探究蛋白酶与肽之间的相互作用，进而指导此类肽传感器的设计，并阐明引发上述同时结合事件的分子机制。该方法旨在推动无需依赖底物切割、且无需多步洗涤步骤的新型酶检测方法的开发。