开发新型荧光探针作为分子传感器是理解分子机制的关键一步。基于 BODIPY 的探针因其高荧光量子产率、光稳定性和可调谐吸收/发射波长而提供多功能性。在这里，我们报告了一种新型 7-azaindole-BODIPY 衍生物的合成和评估，用于探测疏水蛋白以及蛋白质错误折叠和聚集。在有机溶剂中，该化合物显示出两种有效相互转换的发射激发态。在水性环境中，它形成具有独特光物理性质的分子聚集体。 7-azaindole-BODIPY 衍生物的复杂光物理学被探索用于传感应用。在白蛋白存在的情况下，该化合物在疏水蛋白区域稳定，显着增加其荧光发射强度和寿命。类似的效果会在蛋白质聚集体存在时发生，但在胃蛋白酶、DNA、Ficoll 40 和椰子油等其他大分子中则不会。与该化合物孵育的乳腺癌 (MCF-7) 和肺癌 (A549) 癌细胞的荧光寿命成像显微镜 (FLIM) 和双光子荧光显微镜在氧化应激下显示出更长的荧光寿命和更高的发射强度。同步加速器FTIR显微光谱证实观察到的光物理变化是由于氧化应激引起的蛋白质错误折叠和聚集造成的。这些发现表明，该化合物可以作为荧光探针来监测氧化应激引发的蛋白质错误折叠和聚集。

The development of new fluorescent probes as molecular sensors is a critical step for the understanding of molecular mechanisms. BODIPY-based probes offer versatility due to their high fluorescence quantum yields, photostability, and tunable absorption/emission wavelengths. Here, we report the synthesis and evaluation of a novel 7-azaindole-BODIPY derivative to probe hydrophobic proteins as well as protein misfolding and aggregation. In organic solvents, this compound shows two efficiently interconverting emissive excited states. In aqueous environments, it forms molecular aggregates with unique photophysical properties. The complex photophysics of the 7-azaindole-BODIPY derivative was explored for sensing applications. In the presence of albumin, the compound is stabilized in hydrophobic protein regions, significantly increasing its fluorescence emission intensity and lifetime. Similar effects occur in the presence of protein aggregates but not with other macromolecules like pepsin, DNA, Ficoll 40, and coconut oil. Fluorescence lifetime imaging microscopy (FLIM) and two-photon fluorescence microscopy on breast (MCF-7) and lung (A549) cancer cells incubated with this compound display longer fluorescence lifetimes and higher emission intensity under oxidative stress. Synchrotron FTIR micro spectroscopy confirmed that the photophysical changes observed were due to protein misfolding and aggregation caused by the oxidative stress. These findings demonstrate that this compound can serve as a fluorescent probe to monitor protein misfolding and aggregation triggered by oxidative stress.