Nonconventional biomacromolecular luminogens have attracted extensive interest due to their fundamental importance and potential applications in diverse areas. To explore novel luminogens and, moreover, to gain deeper insights into their emission mechanism, we study the emission behaviors of sodium alginate (SA), a natural anionic polysaccharide composed of mannuronic (M) and guluronic acids (G). We find that the luminescence from aqueous SA solutions exhibits distinct concentration enhanced emission and aggregation-induced emission (AIE) characteristics. Meanwhile, the ratio of M/G also matters. Rheological measurements reveal the distinct regimes of the solutions, which are consistent with the observed emission, indicative of strong association between the chain entanglement and emission. Moreover, we observe persistent room temperature phosphorescence (RTP) in the amorphous SA solids, which is a rare case even in pure organic aromatic luminogens. Such unique emission can be remarkably enhanced via coordination with Ca ions. These emission behaviors can be well rationalized by the clustering-triggered emission (CTE) mechanism. Namely, the emission is caused by the electron cloud overlap due to the clustering of oxygen atoms and carboxylate units, together with conformation rigidification. Owing to its biocompatibility, intrinsic emission, and, moreover, persistent RTP, SA shows great potential for anticounterfeiting, encryption, intracellular imaging, and so on.
Herein, we demonstrate a ternary
ionic hydrogel sensor consisting of tannic acid, sodium alginate,
and covalent cross-linked polyacrylamide as skin-mountable and wearable
sensors. Based on the multiple weak H-bonds and synergistic effects
between the three components, the as-prepared hybrid hydrogel exhibits
ultrastretchability with high elasticity, good self-healing, excellent
conformability, and high self-adhesiveness to diverse substrates both
in air and underwater. More importantly, the ternary hydrogel exhibits
high strain sensitivity especially under subtle strains with a gauge
factor of 2.0, which is close to the theoretical value of the ionic
hydrogel sensors; an extremely large workable range of strain (0.05–2100%);
and a low operating voltage 0.07 V. Consequently, the sensor demonstrates
superior sensing performance for real-time monitoring of the large
and subtle human motions, including limb motions, swallowing, smiling,
and wrist pulse. Therefore, it is believed that the STP hydrogel has
great potential applications in health monitoring, smart wearable
devices, and soft robots.
A strategy towards efficient mechanochromic luminogens with high contrast is developed. The twisted propeller-like conformations and effective intermolecular interactions not only endow the luminogens with AIE characteristics and high efficiency in the crystalline state, but also render them to undergo conformational planarization and disruption in intermolecular interactions upon mechanical stimuli, resulting in remarkable changes in emission wavelength and efficiency.
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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