4.7 Article

Regulation on the aggregation-induced emission (AIE) of DNA-templated silver nanoclusters by BSA and its hydrolysates

Journal

JOURNAL OF COLLOID AND INTERFACE SCIENCE
Volume 505, Issue -, Pages 577-584

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jcis.2017.06.033

Keywords

Silver nanocluster; Aggregation-induced emission; BSA; Hydrolysis; Regulation

Funding

  1. NSFC [21373101, 91027027, 21003061]
  2. Natural Science Foundation of Jilin Province [20160101293JC]
  3. State Key Laboratory of Supramolecular Structure and Materials, Jilin University

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The aggregation-induced emission (ALE) phenomenon of the metal nanoclusters (NCs) has been discovered quite recently, which is considered to be creative to improve the optical properties of NCs upon ligand aggregation. In the present study, we report an AIE system for double-stranded DNA-templated silver nanoclusters (AgNCs-dsDNA) by using bovine serum albumin (BSA) in solution, which induce a moderate emission enhancement of AgNCs (5-fold) and a blue-shift through a loosen interaction. In addition, significant luminescence enhancement (30-fold) is further stimulated by the addition of digestive enzyme to the system by altering the surface structure of the aggregated particles. The processes are observed directly through transmission electron microscopy (TEM), where the dispersed AgNCs spheres are aggregated in a large incompact sheet-like film by BSA; while further trypsin addition lead them into larger particles (>50 nm) with higher density. And the intrinsic mechanism is explained well by UV-vis absorption and time-resolved luminescence spectra. The observed luminescence enhancement in step-II is attributed to the AIE through stronger interaction between the hydrolysates of BSA and the ligand dsDNA. Therefore, the optical properties of AgNCs-dsDNA are regulated well by the addition of BSA and trypsin in different amounts, which relates directly to the degree of aggregation and can be extended to other metal nanoclusters by employing the pairs of protein and related enzyme. (C) 2017 Elsevier Inc. All rights reserved.

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