کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7234059 | 1470983 | 2013 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Fluorescent proteins as biosensors by quenching resonance energy transfer from endogenous tryptophan: Detection of nitroaromatic explosives
ترجمه فارسی عنوان
پروتئین های فلورسنت به عنوان بیوسنسورها با رها کردن انتقال انرژی رزونانس از تریپتوفان درونی: تشخیص مواد منفجره نیترواروما
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی
Ensuring domestic safety from terrorist attack is a daunting challenge because of the wide array of chemical agents that must be screened. A panel of purified fluorescent protein isoforms (FPs) was screened for the ability to detect various explosives, explosive simulants, and toxic agents. In addition to their commonly used visible excitation wavelengths, essentially all FPs can be excited by UV light at 280Â nm. Ultraviolet illumination excites electrons in endogenous tryptophan (W) residues, which then relax by Förster Resonance Energy Transfer (FRET) to the chromophore of the FP, and thus the FPs emit with their typical visible spectra. Taking advantage of the fact that tryptophan excitation can be quenched by numerous agents, including nitroaromatics like TNT and nitramines like RDX, it is demonstrated that quenching of visible fluorescence from UV illumination of FPs can be used as the basis for detecting these explosives and explosive degradation products. This work provides the foundation for production of an array of genetically-modified FPs for in vitro biosensors capable of rapid, simultaneous, sensitive and selective detection of a wide range of explosive or toxic agents.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biosensors and Bioelectronics - Volume 48, 15 October 2013, Pages 251-257
Journal: Biosensors and Bioelectronics - Volume 48, 15 October 2013, Pages 251-257
نویسندگان
Alexa Gingras, Joseph Sarette, Evan Shawler, Taeyoung Lee, Steve Freund, Eric Holwitt, Barry W. Hicks,