@article {https://doi.org/10.1002/adma.202304410,
	title = {Modular Aptamer Switches for the Continuous Optical Detection of Small-Molecule Analytes in Complex Media},
	journal = {Advanced Materials},
	volume = {36},
	number = {1},
	year = {2024},
	pages = {2304410},
	abstract = {Abstract Aptamers are a promising class of affinity reagents because signal transduction mechanisms can~be built into the reagent, so that they can directly produce a physically measurable output signal upon target binding. However, endowing the signal transduction functionality into an aptamer remains a trial-and-error process that can compromise its affinity or specificity and typically requires knowledge of the ligand binding domain or its structure. In this work, a design architecture that can convert an existing aptamer into a {\textquotedblleft}reversible aptamer switch{\textquotedblright} whose kinetic and thermodynamic properties can be tuned without a priori knowledge of the ligand binding domain or its structure is described. Finally, by combining these aptamer switches with evanescent-field-based optical detection hardware that minimizes sample autofluorescence, this study demonstrates the first optical biosensor system that can continuously measure multiple biomarkers (dopamine and cortisol) in complex samples (artificial cerebrospinal fluid and undiluted plasma) with second and subsecond-scale time responses at physiologically relevant concentration ranges.},
	keywords = {aptamer switches, biomedical probes, BIOSENSOR, functional materials, real-time detection},
	doi = {https://doi.org/10.1002/adma.202304410},
	url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/adma.202304410},
	author = {Hariri, Amani A. and Cartwright, Alyssa P. and Dory, Constantin and Gidi, Yasser and Yee, Steven and Thompson, Ian A. P. and Fu, Kaiyu X. and Yang, Kiyoul and Wu, Diana and Maganzini, Nicol{\`o} and Feagin, Trevor and Young, Brian E. and Afshar, Behrad Habib and Eisenstein, Michael and Digonnet, Michel J. F. and Vuckovic, Jelena and Soh, H. Tom}
}
@article {1007,
	title = {High affinity DNAzyme-based ligands for transition metal cations - a prototype sensor for Hg2+},
	journal = {Organic \& Biomolecular Chemistry},
	volume = {2},
	number = {3},
	year = {2004},
	note = {ISI Document Delivery No.: 776YCTimes Cited: 32Cited Reference Count: 47},
	month = {Feb},
	pages = {307-312},
	type = {Article},
	abstract = {Inspired by recent interest in DNAzymes as transition metal ion sensors, a survey of the effects of various transition metals on the intramolecular cleavage rate of an imidazole modified, M2+-independent, self-cleaving "9(25)-11" DNA is reported. In particular, 9(25)-11 activity was strongly inhibited by Hg2+ (K-d(APP) = 110 +/- 9 nM). It is postulated that the affinity and selectivity of 9(25)-11 for Hg2+ stems from the fact that this synthetically modified DNAzyme contains imidazoles. This study demonstrates the utility of modified nucleotides in developing DNAzyme sensors for metals ions, especially those for which unmodified nucleic acids might not serve as inherently good ligands.},
	keywords = {2-STEP MECHANISM, BIOSENSOR, CATALYTIC REPERTOIRE, CLEAVING DNA ENZYME, IMIDAZOLYL FUNCTIONALITIES, MERCURIC ION, MERCURY(II), NUCLEIC-ACIDS, NUCLEOSIDES, SELECTION},
	isbn = {1477-0520},
	url = {<Go to ISI>://000189146100008},
	author = {Thomas, J. M. and Ting, R. and Perrin,David M.}
}
@article {3480,
	title = {AN AUTOCLAVABLE GLUCOSE BIOSENSOR FOR MICROBIAL FERMENTATION MONITORING AND CONTROL},
	journal = {Biotechnology and Bioengineering},
	volume = {46},
	number = {6},
	year = {1995},
	note = {ISI Document Delivery No.: QY630Times Cited: 16Cited Reference Count: 49},
	month = {Jun},
	pages = {514-524},
	type = {Article},
	abstract = {The design, construction, and characterization of a prototype-regenerable glucose biosensor based on the reversible immobilization of glucose oxidase (GOx) using cellulose binding domain (CBD) technology is described. GOx, chemically linked to CBD, is immobilized by binding to a cellulose matrix on the sensor-indicating electrode. Enzyme immobilization can be reversed by perfusing the cellulose matrix with a suitable eluting solution. An autoclavable sensor membrane system is employed which is shown to be practical for use in real microbial fermentations. The prototype glucose biosensor was used without failure or deterioration during fed-batch fermentations of Escherichia coli reaching a maximum cell density of 85 g (dry weight)/L. Medium glucose concentration based on sensor output correlated closely with off-line glucose analysis and was controlled manually at 0.44 +/- 0.2 g/L for 2 h based on glucose sensor output. The sensor enzyme component could be eluted and replaced without interrupting the fermentation. To our knowledge, no other in situ biosensor has been used for such an extended period of time in such a high-cell-density fermentation. (C) 1995 John Wiley \& Sons, Inc.},
	keywords = {(CBD), AMPEROMETRIC BIOSENSORS, BATCH, BIOSENSOR, CELLULOSE BINDING DOMAIN, CELLULOSE-BINDING DOMAIN, ELECTROCHEMICAL DETECTOR, ENZYME ELECTRODE, ESCHERICHIA-COLI, FERMENTATION MONITORING, FLOW-INJECTION ANALYSIS, GLUCOSE BIOSENSOR, GLUCOSE OXIDASE, OPTIMIZATION, OXIDASE ELECTRODE, OXYGEN},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1995QY63000003},
	author = {Phelps, M. R. and Hobbs, J. B. and Kilburn, D. G. and Turner, R. F. B.}
}
