生物分子
费斯特共振能量转移
纳米技术
适体
计算生物学
化学
生物传感器
生物过程
生化工程
生物
材料科学
荧光
分子生物学
工程类
物理
古生物学
量子力学
作者
Eugene M. Obeng,Elvina Clarie Dullah,Nur Syahadatain Abdul Razak,Michael K. Danquah,Cahyo Budiman,Clarence M. Ongkudon
出处
期刊:Journal of biological methods
[Journal of Biological Methods]
日期:2017-04-28
卷期号:4 (2): 1-1
被引量:3
标识
DOI:10.14440/jbm.2017.172
摘要
Endotoxin has been one of the topical chemical contaminants of major concern to researchers, especially in the field of bioprocessing. This major concern of researchers stems from the fact that the presence of Gram-negative bacterial endotoxin in intracellular products is unavoidable and requires complex downstream purification steps. For instance, endotoxin interacts with recombinant proteins, peptides, antibodies and aptamers and these interactions have formed the foundation for most biosensors for endotoxin detection. It has become imperative for researchers to engineer reliable means/techniques to detect, separate and remove endotoxin, without compromising the quality and quantity of the end-product. However, the underlying mechanism involved during endotoxin-biomolecule interaction is still a gray area. The use of quantitative molecular microscopy that provides high resolution of biomolecules is highly promising, hence, may lead to the development of improved endotoxin detection strategies in biomolecule preparation. Förster resonance energy transfer (FRET) spectroscopy is one of the emerging most powerful tools compatible with most super-resolution techniques for the analysis of molecular interactions. However, the scope of FRET has not been well-exploited in the analysis of endotoxin-biomolecule interaction. This article reviews endotoxin, its pathophysiological consequences and the interaction with biomolecules. Herein, we outline the common potential ways of using FRET to extend the current understanding of endotoxin-biomolecule interaction with the inference that a detailed understanding of the interaction is a prerequisite for the design of strategies for endotoxin identification and removal from protein milieus.
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