Lead-halide hybrid perovskites (RNHPbX, X = halide, e.g., Cl, Br, I; R = organic moiety) show promise for next-generation optoelectronic devices due to their simple synthesis routes, strong light absorption, and high photoluminescence quantum yield. However, postsynthetic halide exchange in lead-halide perovskites poses a challenge for the functionality of many perovskite devices. For example, in all-perovskite heterostructures, halide diffusion results in the formation of undesired mixed alloys rather than sharp interfaces required for many optoelectronic applications. To address this issue, we incorporated lysine molecules, one of the 20 common amino acids, into a hybrid perovskite MAPbBr (MA = CHNH) host and investigated their impact on the host's ability to undergo postsynthetic halide exchange. We immersed lysine-incorporated MAPbBr crystals in solutions containing Cl or I for varying durations and analyzed subsequent halide exchange-related changes using ion chromatography, high-resolution powder X-ray diffraction, and photoluminescence spectroscopy. Our findings unanimously indicate that incorporated lysine significantly impedes postsynthetic Cl and I diffusion into bulk MAPbBr. Our new bioinspired approach opens a route toward mitigating postsynthetic halide exchange in lead-halide hybrid perovskites and improving the suitability of perovskite devices for optoelectronic applications.

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http://dx.doi.org/10.1021/acsami.4c22194DOI Listing

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