Protein immobilization and fluorescence quenching on polydopamine thin films
Protein immobilization and fluorescence quenching on polydopamine thin films
复制标题
聚多巴胺薄膜上的蛋白质固定和荧光猝灭
DOI：
10.1016/j.jcis.2016.05.042
复制
发表时间：
2016-09-01
影响因子：
9.9
通讯作者：
Hu, Weihua
中科院分区：
文献类型：
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作者：
Chen, Daqun;Zhao, Lei;Hu, Weihua
贻贝激发的聚多巴胺(PDA)膜作为一种用于生物分子固定的多功能涂层，在各种生物相关设备中引起了极大的兴趣。然而，关于蛋白质和PDA膜之间相互作用的细节仍然不清楚。尤其是蛋白质在PDA膜上的固定化，尽管它在各个领域都是至关重要的，但人们对它的了解非常有限。如果考虑到相当多的方法(例如，不同的氧化剂、缓冲液pH、生长时间、生长介质等)，情况就更复杂了。已经被开发用于生长PDA薄膜。本工作利用实时无标记表面等离子体共振(SPR)技术系统地研究了蛋白质在PDA膜上的吸附。探讨了蛋白质与PDA相互作用的动力学，研究了缓冲液pH值和沉淀介质对蛋白质附着的影响。将荧光蛋白质微阵列进一步印制在PDA涂布的玻片上进行定量研究，并结合SPR数据揭示了PDA薄膜有趣的荧光猝灭现象。这项工作可能会加深我们对PDA-蛋白质相互作用的理解，并为在各种生物相关应用中有效地将蛋白质附着在PDA薄膜上提供有价值的指导。(C)2016 Elsevier Inc.保留所有权利。
Mussel inspired polydopamine (PDA) film has attracted great interest as a versatile functional coating for biomolecule immobilization in various bio-related devices. However, the details regarding the interaction between a protein and PDA film remain unclear. Particularly, there is very limited knowledge regarding the protein immobilization on PDA film, even though it is of essential importance in various fields. The situation is even more complicated if considering the fact that quite a number of approaches (e.g., different oxidizing reagent, buffer pH, grown time, grown media, etc.) have been developed to grow PDA films. In this work, protein attachment on PDA film was systematically investigated by using the real-time and label-free surface plasmon resonance (SPR) technique. The kinetics of protein-PDA interaction was explored and the influence of buffer pH and deposition media on the protein attachment was studied. Fluorescent protein microarray was further printed on PDA-coated glass slides for quantitative investigations and together with SPR data, the interesting fluorescence quenching phenomenon of PDA film was revealed. This work may deepen our understanding on the PDA-protein interaction and offer a valuable guide for efficient protein attachment on PDA film in various bio-related applications. (C) 2016 Elsevier Inc. All rights reserved.