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Reevaluating Protein Photoluminescence: Remarkable Visible Luminescence upon Concentration and Insight into the Emission Mechanism.

Qian WangXueyu DouXiaohong ChenZihao ZhaoShuang WangYunzhong WangKunyan SuiYeqiang TanYongyang GongYongming ZhangWang Zhang Yuan
Published in: Angewandte Chemie (International ed. in English) (2019)
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.
Keyphrases
  • amino acid
  • room temperature
  • quantum dots
  • solid state
  • light emitting
  • healthcare
  • energy transfer
  • air pollution
  • protein protein
  • particulate matter
  • ionic liquid
  • optical coherence tomography