Spontaneous decoration of ionic compounds at perovskite interfaces to achieve 23.38% efficiency with 85% fill factor in NiO_X-based perovskite solar cells

Inorganic hole transport materials, particularly NiO_X, have shown considerable promise in boosting the efficiency and stability of perovskite solar cells. However, a major barrier to commercialization of NiO_X-based perovskite solar cells with positive-intrinsic-negative architectures is their direct contact with the absorbing layer, which can lead to losses of photovoltage and fill factor. Furthermore, highly positive under-coordinated Ni cations degrade the perovskite at the interface. Here, we address these issues with the use of an ionic compound(QAPyBF_(4)) as an additive to passivate defects throughout the perovskite layer and improve carrier conduction and interactions with under-coordinated Ni cations. Specifically,the highly electronegative inorganic anion [BF_(4)]~- interacts with the NiO_x/perovskite interface to passivate under-coordinated cations(Ni^(≥3+)). Accordingly, the decorated cells achieved a power conversion efficiency of 23.38% and a fill factor of 85.5% without a complex surface treatment or NiO_X doping.

Application of StrucGP in medical immunology:site-specific N-glycoproteomic analysis of macrophages

The structure of N-glycans on specific proteins can regulate innate and adaptive immunity via sensing environmental signals.Meanwhile,the structural diversity of N-glycans poses analytical challenges that limit the exploration of specific glycosylation functions.In this work,we used THP-1-derived macrophages as examples to show the vast potential of a N-glycan structural interpretation tool StrucGP in N-glycoproteomic analysis.The intact glycopeptides of macrophages were enriched and analyzed using mass spectrometry(MS)-based glycoproteomic approaches,followed by the large-scale mapping of site-specific glycan structures via StrucGP.Results revealed that bisected GlcNAc,core fucosylated,and sialylated glycans(e.g.,HexNAc4Hex5Fuc1Neu5Ac1,N4H5F1S1)were increased in M1 and M2 macrophages,especially in the latter.The findings indicated that these structures may be closely related to macrophage polarization.In addition,a high level of glycosylated PD-L1 was observed in M1 macrophages,and the LacNAc moiety was detected at Asn-192 and Asn-200 of PD-L1,and Asn-200 contained Lewis epitopes.The precision structural interpretation of site-specific glycans and subsequent intervention of target glycoproteins and related glycosyltransferases are of great value for the development of new diagnostic and therapeutic approaches for different diseases.