Photodetection in the visible and near-infrared (NIR) spectral regions offers a wide range of applications, such as image arrays of high pixel density and artificial intelligence. In this work, broadband organic photodiodes (OPDs) are developed with performance comparable to that of crystalline silicon-based commercial devices. Through the strategy of combining an NIR-absorbing non-fullerene acceptor and a thick junction, the resulting devices show significantly improved performance parameters, with a suppressed dark current density of 0.35 nA/cm2, an enhanced spectral response covering 300–1000 nm, and external quantum efficiency over 60% el/ph. Owing to the low dark current noise and high responsivity to NIR wavelengths, an unexpectedly high specific detectivity of 5.1 × 1013 Jones at 930 nm is obtained together with a linear dynamic range of 157  dB and a −3  dB cutoff frequency of 4.5  kHz. These results reveal that the NIR OPD has great potential for 2D and 3D imaging applications with a high frame rate and multiple band selection.

F-box and WD repeat domain-containing 7 (FBW7), the substrate-binding subunit of E3 ubiquitin ligase SCF FBW7 (a complex of SKP1, cullin-1 and FBW7), plays important roles in various physiological and pathological processes. Although FBW7 is required for vascular development, its function in the endothelium remains to be investigated. In this study, we show that FBW7 is an important regulator of endothelial functions, including angiogenesis, leukocyte adhesion and the endothelial barrier integrity. Using RNA interference, we found that the depletion of FBW7 markedly impairs angiogenesis in vitro and in vivo. We identified the zinc finger transcription factor Krüppel-like factor 2 (KLF2) as a physiological target of FBW7 in endothelial cells. Knockdown of FBW7 expression resulted in the accumulation of endogenous KLF2 protein in endothelial cells. FBW7-mediated KLF2 destruction was shown to depend on the phosphorylation of KLF2 via glycogen synthase kinase-3 (GSK3) at two conserved phosphodegrons. Mutating these phosphodegron motifs abolished the FBW7-mediated degradation and ubiquitination of KLF2. The siRNAmediated knockdown of FBW7 showed that KLF2 is an essential target of FBW7 in the regulation of endothelial functions. Moreover, FBW7-mediated KLF2 degradation was shown to be critical for angiogenesis in teratomas and in zebrafish development. Taken together, our study suggests a role for FBW7 in the processes of endothelial cell migration, angiogenesis, inflammation and barrier integrity, and provides novel insights into the regulation of KLF2 stability in vivo.

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