| pubmed-article:20174715 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20174715 | lifeskim:mentions | umls-concept:C1317973 | lld:lifeskim |
| pubmed-article:20174715 | lifeskim:mentions | umls-concept:C0183683 | lld:lifeskim |
| pubmed-article:20174715 | lifeskim:mentions | umls-concept:C0344211 | lld:lifeskim |
| pubmed-article:20174715 | lifeskim:mentions | umls-concept:C1521721 | lld:lifeskim |
| pubmed-article:20174715 | lifeskim:mentions | umls-concept:C0183210 | lld:lifeskim |
| pubmed-article:20174715 | lifeskim:mentions | umls-concept:C0599013 | lld:lifeskim |
| pubmed-article:20174715 | lifeskim:mentions | umls-concept:C1171411 | lld:lifeskim |
| pubmed-article:20174715 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:20174715 | pubmed:dateCreated | 2010-2-22 | lld:pubmed |
| pubmed-article:20174715 | pubmed:abstractText | Electrochemical aptamer-based (E-AB) sensors have emerged as a promising and versatile new biosensor platform. Combining the generality and specificity of aptamer-ligand interactions with the selectivity and convenience of electrochemical readouts, this approach affords the detection of a wide variety of targets directly in complex, contaminant-ridden samples, such as whole blood, foodstuffs and crude soil extracts, without the need for exogenous reagents or washing steps. Signaling in this class of sensors is predicated on target-induced changes in the conformation of an electrode-bound probe aptamer that, in turn, changes the efficiency with which a covalently attached redox tag exchanges electrons with the interrogating electrode. Aptamer selection strategies, however, typically do not select for the conformation-switching architectures, and as such several approaches have been reported to date by which aptamers can be re-engineered such that they undergo the binding-induced switching required to support efficient E-AB signaling. Here, we systematically compare the merits of these re-engineering approaches using representative aptamers specific to the small molecule adenosine triphosphate and the protein human immunoglobulin E. We find that, while many aptamer architectures support E-AB signaling, the observed signal gain (relative change in signal upon target binding) varies by more than two orders of magnitude across the various constructs we have investigated (e.g., ranging from -10% to 200% for our ATP sensors). Optimization of the switching architecture is thus an important element in achieving maximum E-AB signal gain and we find that this optimal geometry is specific to the aptamer sequence upon which the sensor is built. | lld:pubmed |
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| pubmed-article:20174715 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20174715 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20174715 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20174715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20174715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20174715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20174715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20174715 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20174715 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:20174715 | pubmed:issn | 1364-5528 | lld:pubmed |
| pubmed-article:20174715 | pubmed:author | pubmed-author:PlaxcoKevin... | lld:pubmed |
| pubmed-article:20174715 | pubmed:author | pubmed-author:WhiteRyan JRJ | lld:pubmed |
| pubmed-article:20174715 | pubmed:author | pubmed-author:RoweAaron AAA | lld:pubmed |
| pubmed-article:20174715 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20174715 | pubmed:volume | 135 | lld:pubmed |
| pubmed-article:20174715 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20174715 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20174715 | pubmed:pagination | 589-94 | lld:pubmed |
| pubmed-article:20174715 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:20174715 | pubmed:meshHeading | pubmed-meshheading:20174715... | lld:pubmed |
| pubmed-article:20174715 | pubmed:meshHeading | pubmed-meshheading:20174715... | lld:pubmed |
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| pubmed-article:20174715 | pubmed:meshHeading | pubmed-meshheading:20174715... | lld:pubmed |
| pubmed-article:20174715 | pubmed:meshHeading | pubmed-meshheading:20174715... | lld:pubmed |
| pubmed-article:20174715 | pubmed:meshHeading | pubmed-meshheading:20174715... | lld:pubmed |
| pubmed-article:20174715 | pubmed:meshHeading | pubmed-meshheading:20174715... | lld:pubmed |
| pubmed-article:20174715 | pubmed:meshHeading | pubmed-meshheading:20174715... | lld:pubmed |
| pubmed-article:20174715 | pubmed:meshHeading | pubmed-meshheading:20174715... | lld:pubmed |
| pubmed-article:20174715 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20174715 | pubmed:articleTitle | Re-engineering aptamers to support reagentless, self-reporting electrochemical sensors. | lld:pubmed |
| pubmed-article:20174715 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, CA 93106, USA. | lld:pubmed |
| pubmed-article:20174715 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20174715 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:20174715 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
