光致发光
发光
机制(生物学)
化学
材料科学
化学物理
纳米技术
生物物理学
生物
量子力学
光电子学
物理
作者
Qian Wang,Xueyu Dou,Xiaohong Chen,Zihao Zhao,Shuang Wang,Yunzhong Wang,Kunyan Sui,Yeqiang Tan,Yongyang Gong,Yongming Zhang,Wang Zhang Yuan
标识
DOI:10.1002/anie.201906226
摘要
Abstract It is a textbook knowledge that protein photoluminescence stems from the three aromatic amino acid residues of tryptophan(Trp), tyrosine (Tyr), and phenylalanine (Phe), with predominant contributions from Trp. Recently, inspired by the intrinsic emission of nonaromatic amino acids and poly(amino acids) in concentrated solutions and solids, we revisited protein light emission using bovine serum albumin (BSA) as a model. BSA is virtually nonemissive in dilute solutions (≤0.1 mg mL −1 ), but highly luminescent upon concentration or aggregation, showing unique concentration‐enhanced emission and aggregation‐induced emission (AIE) characteristics. Notably, apart from well‐documented UV luminescence, bright blue emission is clearly observed. Furthermore, persistent room‐temperature phosphorescence ( p ‐RTP) is achieved even in the amorphous solids under ambient conditions. This visible emission can be rationalized by the clustering‐triggered emission (CTE) mechanism. These findings not only provide an in‐depth understanding of the emissive properties of proteins, but also hold strong implications for further elucidating the basis of tissue autofluorescence.
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